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L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
bi uni uni bi ping pong mechanism, recombinant histidinol dehydrogenase
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
fast reversible oxidation of L-histidanol, followed by slow irreversible hydride transfer from the intermediate L-histidinal
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
also oxidizes L-histidinal
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L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
reaction mechanism, amino acid residues Glu326 and His327 are involved in catalysis
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
bi uni uni bi ping-pong enzyme mechanism for MtHisD-catalyzed chemical reaction, involves abstraction of the hydroxyl group proton of L-histidinol by His336 and concomitant hydride transfer from the reactive carbon (carbon bound to the hydroxyl group that upon hydride transfer adopts the sp2 configuration) to NAD+, forming L-histidinaldehyde and transiently protonated His336
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
enzyme HisD from Mycobacterium tuberculosis follows a bi uni uni bi ping-pong mechanism in which L-histidinol is the first substrate to bind and L-histidine the last product to dissociate, the amino acid side chains of His336 and Glu335 are likely involved in catalysis and/or substrate binding
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
-
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
enzyme HisD from Mycobacterium tuberculosis follows a bi uni uni bi ping-pong mechanism in which L-histidinol is the first substrate to bind and L-histidine the last product to dissociate, the amino acid side chains of His336 and Glu335 are likely involved in catalysis and/or substrate binding
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-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
-
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
bi uni uni bi ping-pong enzyme mechanism for MtHisD-catalyzed chemical reaction, involves abstraction of the hydroxyl group proton of L-histidinol by His336 and concomitant hydride transfer from the reactive carbon (carbon bound to the hydroxyl group that upon hydride transfer adopts the sp2 configuration) to NAD+, forming L-histidinaldehyde and transiently protonated His336
-
-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
the enzyme catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine using a bi-uni-uni-bi ping pong kinetic mechanism
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-
L-histidinol + 2 NAD+ + H2O = L-histidine + 2 NADH + 2 H+
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L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
L-histidinol + NAD+
L-histidinal + NADH + H+
additional information
?
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L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
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L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
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?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
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?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
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?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
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?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
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ir
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
enzyme is responsible for catalysis of the terminal step in L-histidine biosynthesis, being performed in 2 sequential reactions via the intermediate L-histidinal
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ir
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
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?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
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?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
ir
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
ir
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
-
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
part of L-histidine biosynthesis
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
ir
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
two steps: NAD+-dependent oxidations of L-histidinol to L-histidinaldehyde and subsequently to L-histidine
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
two steps: NAD+-dependent oxidations of L-histidinol to L-histidinaldehyde and subsequently to L-histidine
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
the enzyme is highly specific for histidinol and NAD+
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
via L-histidinaldehyde intermediate
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
NAD+- and Zn+-dependent conversion of L-histidinol to L-histidine through an L-histidinaldehyde intermediate, leading to the concomitant reduction of 2 NAD+ molecules
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-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
NAD+- and Zn+-dependent conversion of L-histidinol to L-histidine through an L-histidinaldehyde intermediate, leading to the concomitant reduction of 2 NAD+ molecules
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
via L-histidinaldehyde intermediate
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
the enzyme is highly specific for histidinol and NAD+
-
-
?
L-histidinol + NAD+
L-histidinal + NADH + H+
-
-
-
-
ir
L-histidinol + NAD+
L-histidinal + NADH + H+
-
enzyme is responsible for catalysis of the terminal step in L-histidine biosynthesis, being performed in 2 sequential reactions via the intermediate L-histidinal
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ir
L-histidinol + NAD+
L-histidinal + NADH + H+
-
-
-
ir
additional information
?
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active site binding structure for substrates L-histidinol, L-histamine, and L-histidine, NMR study
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?
additional information
?
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ligand-protein interactions in the active site of GcHDH, molecular docking, overview
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?
additional information
?
-
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ligand-protein interactions in the active site of GcHDH, molecular docking, overview
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?
additional information
?
-
imidazole-containing substrate analogues are likely to bind to free enzyme
-
-
?
additional information
?
-
imidazole-containing substrate analogues are likely to bind to free enzyme
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
L-histidinol + NAD+
L-histidinal + NADH + H+
-
enzyme is responsible for catalysis of the terminal step in L-histidine biosynthesis, being performed in 2 sequential reactions via the intermediate L-histidinal
-
-
ir
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
enzyme is responsible for catalysis of the terminal step in L-histidine biosynthesis, being performed in 2 sequential reactions via the intermediate L-histidinal
-
-
ir
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
ir
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinal + NAD+ + H2O
L-histidine + NADH + H+
-
reaction intermediate
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
part of L-histidine biosynthesis
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
ir
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 2 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
via L-histidinaldehyde intermediate
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
via L-histidinaldehyde intermediate
-
-
?
L-histidinol + 2 NAD+ + H2O
L-histidine + 2 NADH + 3 H+
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Ca2+
can partially substitute for Zn2+
Cd2+
-
0.02-0.2 mM, 75% increase
Cd2+
activates, to a higher degree than Zn2+
Cd2+
-
activates, to a higher degree than Zn2+
Cd2+
activates, to a higher degree than Zn2+
Cd2+
activates, to a higher degree than Zn2+
Cd2+
activates, to a higher degree than Zn2+
Cd2+
activates, to a higher degree than Zn2+
Cd2+
activates, to a higher degree than Zn2+
Cd2+
activates, to a higher degree than Zn2+
Co2+
activates less than Zn2+
Co2+
-
activates less than Zn2+
Co2+
activates less than Zn2+
Co2+
activates less than Zn2+
Co2+
activates less than Zn2+
Co2+
activates less than Zn2+
Co2+
activates less than Zn2+
Co2+
activates less than Zn2+
Cu2+
activates less than Zn2+
Cu2+
-
activates less than Zn2+
Cu2+
activates less than Zn2+
Cu2+
activates less than Zn2+
Cu2+
activates less than Zn2+
Cu2+
activates less than Zn2+
Cu2+
activates less than Zn2+
Cu2+
activates less than Zn2+
Mg2+
activates less than Zn2+
Mg2+
-
activates less than Zn2+
Mg2+
activates less than Zn2+
Mg2+
activates less than Zn2+
Mg2+
activates less than Zn2+
Mg2+
activates less than Zn2+
Mg2+
can partially substitute for Zn2+
Mg2+
activates less than Zn2+
Mg2+
activates less than Zn2+
Mn2+
-
-
Mn2+
-
0.5 mM, 26% increase
Mn2+
activates, to a higher degree than Zn2+
Mn2+
-
activates, to a higher degree than Zn2+
Mn2+
activates, to a higher degree than Zn2+
Mn2+
activates, to a higher degree than Zn2+
Mn2+
-
0.5 mM, 165% increase
Mn2+
activates, to a higher degree than Zn2+, which stabilizes the enzyme in its catalytically active form
Mn2+
activates, to a higher degree than Zn2+
Mn2+
best activating divalent cation
Mn2+
activates, to a higher degree than Zn2+
Mn2+
activates, to a higher degree than Zn2+, which stabilizes the enzyme in its catalytically active form
Ni2+
activates less than Zn2+
Ni2+
-
activates less than Zn2+
Ni2+
activates less than Zn2+
Ni2+
activates less than Zn2+
Ni2+
activates less than Zn2+
Ni2+
activates less than Zn2+
Ni2+
activates less than Zn2+
Ni2+
activates less than Zn2+
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
-
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
required, active site-bound, one Zn2+ ion per monomer. The Zn2+ ion plays a crucial role in the proper positioning of the substrate, binding structure, overview
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
-
0.5 mM, 20% increase
Zn2+
binding site structure
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
required, one Zn2+ bound per subunit of the dimer. Zn2+ ion is octahedrally coordinated to Gln267, His270, Asp369, His428, and two ligands from L-histidinol
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
-
essential for activity, one Zn atom per subunit
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. His261 and His418 are candidates for zinc ion ligands, as affinities for metal ions decrease with substitutions at these residues. Binding structure analysis
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
-
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the enzyme is metal-dependent, activity of the apo-enzyme can be rescued by addition of Mn2+, Mg2+, Ca2+, and Zn2+, but not by addition of Cd2+, Co2+ and Ni2+, overview
additional information
-
the enzyme is metal-dependent, activity of the apo-enzyme can be rescued by addition of Mn2+, Mg2+, Ca2+, and Zn2+, but not by addition of Cd2+, Co2+ and Ni2+, overview
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-(naphthalen-2-ylsulfonyl)propanehydrazide
-
-
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(4-methylphenyl)sulfonyl]propanehydrazide
-
-
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
(2S)-2-amino-N'-[(4-bromophenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide
-
-
(3S)-3-amino-1-(2,3,4,5,6-pentafluorophenyloxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(2,3,4,5,6-pentafluorophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(2,4-difluorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-(4-bromophenoxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-(4-bromophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-(4-fluorophenoxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(4-fluorophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-(4-hydroxyphenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
(3S)-3-amino-1-([1,1'-biphenyl]-4-yl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-hydroxy-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-thio-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
-
-
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
(3S)-3-amino-1-[4-(biphenyl-4-ylethynyl)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-[4-(biphenyl-4-ylmethoxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-[4-[(4-bromobenzyl)oxy]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-[4-[(4-butylbenzyl)oxy]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
50% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-1-[4-[(4-tert-butylphenyl)ethynyl]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
30% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-1-[4-[(E)-2-(biphenyl-4-yl)ethenyl]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-methylphenyl)butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[(E)-2-[4-(trifluoromethyl)phenyl]ethenyl]phenyl)butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[[4-(naphthalen-2-yl)benzyl]oxy]phenyl)butan-2-one
-
complete inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)butan-2-one
-
70% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yloxy)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-ylthio)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(p-tolyloxy)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(phenyloxy)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(phenylthio)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(tolylthio)butan-2-one dihydrochloride
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-phenylbutan-2-one
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(2-phenylethyl)phenyl]butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(7-phenylhept-1-yn-1-yl)phenyl]butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(phenylethynyl)phenyl]butan-2-one
-
complete inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(1E)-3-phenylprop-1-en-1-yl]phenyl]butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methoxybenzyl)oxy]phenyl]butan-2-one
-
30% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methylbenzyl)oxy]phenyl]butan-2-one
-
30% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methylphenyl)ethynyl]phenyl]butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-pentylphenyl)ethynyl]phenyl]butan-2-one
-
30% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-phenoxybenzyl)oxy]phenyl]butan-2-one
-
70% inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(E)-2-(4-methylphenyl)ethenyl]phenyl]butan-2-one
-
complete inhibition of pathogen growth in minimal medium at 0.5 mM
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(E)-2-phenylethenyl]phenyl]butan-2-one
-
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
(3S)-3-amino-4-(1H-imidazol-4-yl)butan-2-one
-
(7R)-1,3-diiodo-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
-
weaker inhibitor
(7S)-7-[(2,4-difluorophenyl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
-
(7S)-7-[(4-bromophenyl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
-
(7S)-7-[(4-chlorophenyl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
-
(7S)-7-[(4-methylphenyl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
-
(7S)-7-[([1,1'-biphenyl]-4-yl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
-
(7S)-7-[[4-(7-phenylhept-1-yn-1-yl)phenyl]acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
-
(8S)-8-[2-(biphenyl-4-yl)ethanethioyl]-7,8-dihydroimidazo[1,5-c]pyrimidine-5(6H)-thione
-
(S)-3-amino-1-(4-(benzyloxy)phenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
(S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
(S)-3-amino-1-(4-fluorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-phenoxyphenyl)butan-2-one
-
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yl)butan-2-one
(S)-3-amino-4-(1H-imidazol-4-yl)-1-p-tolylbutan-2-one
-
-
1,10-phenanthroline
54% inhibition at 1 mM, 96% at 5 mM
1,3-diiodo-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
-
2-(2,4-difluorophenyl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
-
-
2-(4-bromophenyl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
-
-
2-(4-chlorophenyl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
-
-
2-(4-methylphenyl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
-
-
2-([1,1'-biphenyl]-4-yl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
-
-
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(4-methoxyphenyl)methylidene]propanehydrazide
-
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(4-methylphenyl)methylidene]propanehydrazide
-
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(4-nitrophenyl)methylidene]propanehydrazide
-
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(4-phenoxyphenyl)methylidene]propanehydrazide
-
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(naphthalen-2-yl)methylidene]propanehydrazide
-
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-phenylmethylidene]propanehydrazide (non-preferred name)
-
2-amino-N'-[(E)-(2-hydroxyphenyl)methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
-
2-amino-N'-[(E)-(4-bromophenyl)methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
-
2-amino-N'-[(E)-(4-chlorophenyl)methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
-
2-amino-N'-[(E)-(4-fluorophenyl)methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
-
2-amino-N'-[(E)-[4-(dimethylamino)phenyl]methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
-
2-[4-(7-phenylhept-1-yn-1-yl)phenyl]-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
-
-
3-(1H-imidazol-4-yl)propanoic acid
-
5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
i.e. RJ-278
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
7-chloro-4-nitro-2,1,3-benzoxadiazole
-
0.1 mM, pseudo first order inactivation, binds to Cys-116 in active site
Ba2+
-
0.5 mM, 35% inhibition
Borate
-
10 mM, 90% inhibition
Cd2+
-
0.1 mM, 33% inhibition
histamine
-
competitive inhibition
imidazole
-
competitive inhibition
imidazole-4-carboxylic acid
-
most active inhibitor
methyl (7R)-1-chloro-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
-
weaker inhibitor
methyl (7S)-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
-
-
methyl (7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
-
-
methyl 1-chloro-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
-
methyl 1-methyl-N-(phenoxycarbonyl)histidinate
-
methyl 3-(1H-imidazol-4-yl)propanoate
methyl N-(ethoxycarbonyl)-1-methyl-L-histidinate
-
-
methyl N-(methoxycarbonyl)-3-methyl-L-histidinate
-
-
methyl N-(methoxycarbonyl)histidinate
-
N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide
Ni2+
-
0.5 mM, 54% inhibition
pyridoxal 5'-phosphate
-
100 mM, 62.5% inhibition, concentration dependent, almost completely reversible
Urea
-
2.2 mM, 50% inhibition, reversible
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
-
-
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
-
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
causes strong in vivo inhibition and growth inhibition
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
-
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
a nanomolar inhibitor, binding structure, overview
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
-
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
-
causes strong in vivo inhibition and growth inhibition
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
-
(S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
growth of cells is inhibited in minimal medium, multiplication of cells in human macrophages is totally abolished. No biological effect in rich medium
(S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
growth of cells is inhibited in minimal medium, multiplication of cells in human macrophages is totally abolished. No biological effect in rich medium
(S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
-
-
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yl)butan-2-one
-
growth of cells is inhibited in minimal medium, multiplication of cells in human macrophages is totally abolished. No biological effect in rich medium
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yl)butan-2-one
-
-
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
most active inhibitor
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
-
Ca2+
-
-
Ca2+
-
0.5 mM, 64% inhibition
Cu2+
-
-
Cu2+
-
0.5 mM, 76% inhibition
EDTA
118% activity at 0.1 mM, 135% at 1 mM, slightly inhibitory above 10 mM
EDTA
-
30 mM, 50% inhibition at pH 7.5
HgCl2
-
0.5 mM, 100% inhibition, 0.05 mM 79% inhibition
HgCl2
-
0.1 mM, 80% inhibition, pH 9.4
methyl 3-(1H-imidazol-4-yl)propanoate
-
-
methyl 3-(1H-imidazol-4-yl)propanoate
-
Mg2+
-
-
Mg2+
-
0.5 mM, 46% inhibition
N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide
-
75% inhibition with one equivalent per subunit
N-(4-dimethylamino-3,5-dinitrophenyl)-maleimide
-
-
p-chloromercuribenzoate
-
0.02 mM, 50% inhibition
p-chloromercuribenzoate
-
75% inhibition with two equivalents per subunit
p-chloromercuribenzoate
-
2.5 mM, 60% inhibition
Zn2+
-
-
Zn2+
-
0.5 mM, 66% inhibition
additional information
exploration of enzyme inhibitors for potential application as novel antimicrobial drugs
-
additional information
-
synthesis and evaluation of alpha-O-arylketones and alpha-S-arylketones derived from histidine
-
additional information
-
exploration of enzyme inhibitors for potential application as antimicrobial drugs
-
additional information
-
design, synthesis and evaluation of 19 potential HDH inhibitors, molecular modeling and docking study, overview
-
additional information
-
synthesis of a family of oxo- and thioxo-imidazo[1,5-c]pyrimidines, potential enzyme inhibitors. These oxo- and thioxo-derivatives can improve dramatically the efficiency of the histidine protection pathway for the synthesis of histidine analogues, overview
-
additional information
exploration of enzyme inhibitors for potential application as novel antimicrobial drugs
-
additional information
exploration of enzyme inhibitors for potential application as novel antimicrobial drugs
-
additional information
exploration of enzyme inhibitors for potential application as novel antimicrobial drugs
-
additional information
-
5% dimethyl sulfoxide or methyl N-[(trifluoromethoxy)carbonyl]-L-histidinate trifluoroacetate fails to exert any growth inhibitory activity
-
additional information
screening of substrate analog inhibitors of histidinol dehydrogenase, and docking analysis of these antifungal agents, overview
-
additional information
-
screening of substrate analog inhibitors of histidinol dehydrogenase, and docking analysis of these antifungal agents, overview
-
additional information
exploration of enzyme inhibitors for potential application as novel antimicrobial drugs
-
additional information
synthesis of hydrazones derived from L-histidine as enzyme inhibitors in the low micromolar range, overview. Molecular docking study and enzyme-inhibitor complex structure analysis
-
additional information
exploration of enzyme inhibitors for potential application as novel antimicrobial drugs. Enzyme inactivation by chelating agents
-
additional information
exploration of enzyme inhibitors for potential application as novel antimicrobial drugs
-
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0.14
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-(naphthalen-2-ylsulfonyl)propanehydrazide
Brucella suis
-
pH 9.2, 30Ā°C
0.16
(2S)-2-amino-3-(1H-imidazol-4-yl)-N'-[(4-methylphenyl)sulfonyl]propanehydrazide
Brucella suis
-
pH 9.2, 30Ā°C
0.025
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
0.07
(2S)-2-amino-N'-[(4-bromophenyl)sulfonyl]-3-(1H-imidazol-4-yl)propanehydrazide
Brucella suis
-
pH 9.2, 30Ā°C
0.0028
(3S)-3-amino-1-(2,3,4,5,6-pentafluorophenyloxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.0192
(3S)-3-amino-1-(2,3,4,5,6-pentafluorophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.01
(3S)-3-amino-1-(2,4-difluorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.19
0.0016
(3S)-3-amino-1-(4-bromophenoxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.006
(3S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.16
0.0028
(3S)-3-amino-1-(4-bromophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.012
(3S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.17
0.0047
(3S)-3-amino-1-(4-fluorophenoxy)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.0031
(3S)-3-amino-1-(4-fluorophenylthio)-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.00004
(3S)-3-amino-1-(4-hydroxyphenyl)-4-(1H-imidazol-4-yl)butan-2-one
Brassica oleracea
pH and temperature not specified in the publication
0.012
(3S)-3-amino-1-([1,1'-biphenyl]-4-yl)-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.20
0.000024
(3S)-3-amino-1-hydroxy-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.0021
(3S)-3-amino-1-thio-4-(1H-imidazol-4-yl)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.000003 - 3
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
40
(3S)-3-amino-1-[4-[(4-butylbenzyl)oxy]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
65
(3S)-3-amino-1-[4-[(4-tert-butylphenyl)ethynyl]phenyl]-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
0.015
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-methylphenyl)butan-2-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.18
65
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[(E)-2-[4-(trifluoromethyl)phenyl]ethenyl]phenyl)butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
30
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[[4-(naphthalen-2-yl)benzyl]oxy]phenyl)butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
30
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-[[4-(trifluoromethyl)benzyl]oxy]phenyl)butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
0.00011
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yloxy)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.0033
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-ylthio)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.00021
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(p-tolyloxy)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.0037
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(phenyloxy)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.0071
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(phenylthio)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.0395
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-(tolylthio)butan-2-one dihydrochloride
Brucella sp.
-
pH 9.2, 30Ā°C, recombinant His6-tagged enzyme
0.001
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-phenylbutan-2-one
Escherichia coli
pH and temperature not specified in the publication
13
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(2-phenylethyl)phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
0.009
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(7-phenylhept-1-yn-1-yl)phenyl]butan-2-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.21
3
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-(phenylethynyl)phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
30
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(1E)-3-phenylprop-1-en-1-yl]phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
20
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methoxybenzyl)oxy]phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
30
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methylbenzyl)oxy]phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
40
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-methylphenyl)ethynyl]phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
8.5
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-pentylphenyl)ethynyl]phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
70
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(4-phenoxybenzyl)oxy]phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
40
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(E)-2-(4-methylphenyl)ethenyl]phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
25
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[(E)-2-phenylethenyl]phenyl]butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
0.000003 - 0.00007
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
0.005
(3S)-3-amino-4-(1H-imidazol-4-yl)butan-2-one
Salmonella enterica subsp. enterica serovar Typhimurium
pH and temperature not specified in the publication
0.0587
(7R)-1,3-diiodo-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
Geotrichum candidum
-
-
0.143
(7S)-7-[(2,4-difluorophenyl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.6
0.098
(7S)-7-[(4-bromophenyl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.3
0.092
(7S)-7-[(4-chlorophenyl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.4
0.113
(7S)-7-[(4-methylphenyl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.5
0.086
(7S)-7-[([1,1'-biphenyl]-4-yl)acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.7
0.175
(7S)-7-[[4-(7-phenylhept-1-yn-1-yl)phenyl]acetyl]-7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.8
0.005
(8S)-8-[2-(biphenyl-4-yl)ethanethioyl]-7,8-dihydroimidazo[1,5-c]pyrimidine-5(6H)-thione
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000003
(S)-3-amino-1-(4-(benzyloxy)phenyl)-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
pH 9.2, 30Ā°C
0.000006
(S)-3-amino-1-(4-bromophenyl)-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
pH 9.2, 30Ā°C
0.000012
(S)-3-amino-1-(4-chlorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
pH 9.2, 30Ā°C
0.000015
(S)-3-amino-1-(4-fluorophenyl)-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
pH 9.2, 30Ā°C
0.000016
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(4-phenoxyphenyl)butan-2-one
Brucella suis
-
pH 9.2, 30Ā°C
0.0000145
(S)-3-amino-4-(1H-imidazol-4-yl)-1-(naphthalen-2-yl)butan-2-one
Brucella suis
-
pH 9.2, 30Ā°C
0.000015
(S)-3-amino-4-(1H-imidazol-4-yl)-1-p-tolylbutan-2-one
Brucella suis
-
pH 9.2, 30Ā°C
0.0587
1,3-diiodo-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
Geotrichum candidum
pH not specified in the publication, temperature not specified in the publication
0.095
2-(2,4-difluorophenyl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.13
0.105
2-(4-bromophenyl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.10
0.074
2-(4-chlorophenyl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.11
0.095
2-(4-methylphenyl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.12
0.005
2-([1,1'-biphenyl]-4-yl)-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.14
0.005
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(4-methoxyphenyl)methylidene]propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.0055
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(4-methylphenyl)methylidene]propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.0025
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(4-nitrophenyl)methylidene]propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.0098
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(4-phenoxyphenyl)methylidene]propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.0011
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-(naphthalen-2-yl)methylidene]propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.029
2-amino-3-(1H-imidazol-4-yl)-N'-[(E)-phenylmethylidene]propanehydrazide (non-preferred name)
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.027
2-amino-N'-[(E)-(2-hydroxyphenyl)methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.0077
2-amino-N'-[(E)-(4-bromophenyl)methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.0024
2-amino-N'-[(E)-(4-chlorophenyl)methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.0024
2-amino-N'-[(E)-(4-fluorophenyl)methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.0091
2-amino-N'-[(E)-[4-(dimethylamino)phenyl]methylidene]-3-(1H-imidazol-4-yl)propanehydrazide
Mycobacterium tuberculosis
pH 7.2, 25Ā°C
0.322
2-[4-(7-phenylhept-1-yn-1-yl)phenyl]-1-[(7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidin-7-yl]ethan-1-one
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.15
0.00317
3-(1H-imidazol-4-yl)propanoic acid
Geotrichum candidum
pH not specified in the publication, temperature not specified in the publication
0.00356
5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylic acid
Geotrichum candidum
pH not specified in the publication, temperature not specified in the publication
0.0242
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
0.0064
imidazole-4-carboxylic acid
Geotrichum candidum
-
-
0.1222
methyl (7R)-1-chloro-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
Geotrichum candidum
-
-
0.532
methyl (7S)-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.2
0.018
methyl (7S)-5-sulfanylidene-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
Brucella suis
-
at 30Ā°C in the presence of 0.05 mM histidinol, 2 mM NAD+ and 0.5 mM MnCl2 in 150 mM sodium glycine buffer at pH 9.9
0.1222
methyl 1-chloro-5-oxo-5,6,7,8-tetrahydroimidazo[1,5-c]pyrimidine-7-carboxylate
Geotrichum candidum
pH not specified in the publication, temperature not specified in the publication
0.0293
methyl 1-methyl-N-(phenoxycarbonyl)histidinate
Geotrichum candidum
pH not specified in the publication, temperature not specified in the publication
0.0052
methyl 3-(1H-imidazol-4-yl)propanoate
0.0293
methyl N-(ethoxycarbonyl)-1-methyl-L-histidinate
Geotrichum candidum
-
-
0.0106
methyl N-(methoxycarbonyl)-3-methyl-L-histidinate
Geotrichum candidum
-
-
0.0106
methyl N-(methoxycarbonyl)histidinate
Geotrichum candidum
pH not specified in the publication, temperature not specified in the publication
0.025
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
Brucella suis
-
pH 9.2, 30Ā°C
0.025
(2S)-2-amino-N'-(biphenyl-4-ylsulfonyl)-3-(1H-imidazol-4-yl)propanehydrazide
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.000003
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
3
(3S)-3-amino-1-[4-(benzyloxy)phenyl]-4-(1H-imidazol-4-yl)butan-2-one
Brucella suis
-
pH and temperature not specified in the publication
0.000003
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
Brucella sp.
-
pH and temperature not specified in the publication
0.00007
(3S)-3-amino-4-(1H-imidazol-4-yl)-1-[4-[4-(phenylethynyl)benzyl]phenyl]butan-2-one
Mycobacterium tuberculosis
pH and temperature not specified in the publication
0.0242
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
Geotrichum candidum
-
-
0.0242
7,8-dihydroimidazo[1,5-c]pyrimidin-5(6H)-one
Geotrichum candidum
pH not specified in the publication, temperature not specified in the publication
0.0052
methyl 3-(1H-imidazol-4-yl)propanoate
Geotrichum candidum
-
-
0.0052
methyl 3-(1H-imidazol-4-yl)propanoate
Geotrichum candidum
pH not specified in the publication, temperature not specified in the publication
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malfunction
-
enzyme inhibition leads to inhibition of intracellular bacterial growth in macrophage infection of the facultative intracellular pathogen
malfunction
a Tn5-mutant affected in hisD is strongly impaired in intramacrophagic replication
malfunction
growth of a hisD mutant auxotrophic for His is restrcted in human THP-1 macrophage-like cells
malfunction
-
a Tn5-mutant affected in hisD is strongly impaired in intramacrophagic replication
-
malfunction
-
growth of a hisD mutant auxotrophic for His is restrcted in human THP-1 macrophage-like cells
-
metabolism
histidinol dehydrogenase mediates the final step in the histidine biosynthetic pathway
metabolism
-
the enzyme catalyzes the last step in histidine biosynthesis
metabolism
-
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
metabolism
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
metabolism
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
metabolism
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
metabolism
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
metabolism
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
metabolism
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis. In the pathogen's bacterial biosynthesis of His is crucial for intracellular growth, the vacuole-borne pathogens have no access to this amino acid produced by the host cell
metabolism
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis. In the pathogen's bacterial biosynthesis of His is crucial for intracellular growth, the vacuole-borne pathogens have no access to this amino acid produced by the host cell
metabolism
the enzyme is involved in the histidine biosynthesis pathway catalyzing catalyzes the last two steps in the histidine biosynthesis pathway, namely the sequential NAD+-dependent oxidations of L-histidinol to L-histidinaldehyde and subsequently to L-histidine
metabolism
reaction mechanism: a proton is withdrawn from the histidinol O atom by Nepsilon of His368 (Base 1) that becomes double-protonated, and one hydride is abstracted by the first NAD+ molecule, and histidinaldehyde is formed. The used NADH dissociates and is replaced by the second NAD+ molecule. A water molecule is activated by Glu367 (Base 2) and performs a nucleophilic attack on the reactive carbon, forming a new C-O bond. Simultaneously, the histidinaldehyde oxygen withdraws the proton back from Nepsilon of His368, resulting in the formation of a gem-diol histidinaldehyde hydrate. In the next step, His368 abstracts a proton from one of the hydroxyl groups of histidinaldehyde hydrate, whereas the second NAD+ removes hydride from the reactive carbon, producing His
metabolism
-
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis. In the pathogen's bacterial biosynthesis of His is crucial for intracellular growth, the vacuole-borne pathogens have no access to this amino acid produced by the host cell
-
metabolism
-
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis. In the pathogen's bacterial biosynthesis of His is crucial for intracellular growth, the vacuole-borne pathogens have no access to this amino acid produced by the host cell
-
metabolism
-
L-histidinol dehydrogenase (HDH, EC 1.1.1.23) is a 4-electron oxidoreductase involved in the last two steps of L-histidine biosynthesis
-
metabolism
-
the enzyme is involved in the histidine biosynthesis pathway catalyzing catalyzes the last two steps in the histidine biosynthesis pathway, namely the sequential NAD+-dependent oxidations of L-histidinol to L-histidinaldehyde and subsequently to L-histidine
-
physiological function
-
the enzyme is essential for intramacrophagic replication
physiological function
-
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
physiological function
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development. The enzyme is essential for infection of the host cell
physiological function
the enzyme is essential for Mycobacterium tuberculosis survival in vitro
physiological function
-
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development. The enzyme is essential for infection of the host cell
-
physiological function
-
the enzyme is essential for Mycobacterium tuberculosis survival in vitro
-
physiological function
-
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
-
physiological function
-
role of the crucial enzyme in intracellular bacteria, overview. The enzyme acts as a HDH as a virulence factor in pathogenic bacteria with intramacrophagic development
-
additional information
molecular homology model building, overview. His336 plays a critical role in both catalysis and L-Hol binding to MtHisD, Tyr129, Tyr223 and His335 residues make contacts with the substrates in the MtHisD enzyme active site, three-dimensional model analysis, overview
additional information
-
molecular homology model building, overview. His336 plays a critical role in both catalysis and L-Hol binding to MtHisD, Tyr129, Tyr223 and His335 residues make contacts with the substrates in the MtHisD enzyme active site, three-dimensional model analysis, overview
additional information
MtHisD is a bifunctional four-electron dehydrogenase enzyme that catalyzes two subsequent reactions, the oxidation of L-Hol and the reduction of two NAD+ molecules,23 with the formation of two intermediaries, L-histidinaldehyde and L-histidindiol. L-histidinaldehyde is very unstable at neutral pH when not bound to HisD
additional information
residues Glu326 and His327 are directly involved in catalysis, the first participating in acid-base catalysis and the second activating a water molecule, active site structure, overview
additional information
-
two identical active sites, one in each subunit of the dimer
additional information
two identical active sites, one in each subunit of the dimer
additional information
two identical active sites, one in each subunit of the dimer
additional information
two identical active sites, one in each subunit of the dimer
additional information
two identical active sites, one in each subunit of the dimer, molecular homology modeling
additional information
two identical active sites, one in each subunit of the dimer, residues His261 and His326 are involved in proton transfers during catalysis
additional information
two identical active sites, one in each subunit of the dimer. The dimer layout resulting in an active site displays a domain swapping between the monomers and allows a complete mapping of the Zn2+ and substrate binding by the involved residues
additional information
two identical active sites, one in each subunit of the dimer. Two histidine residues are critical for the activity, both amino acids are zinc ligands
additional information
-
two identical active sites, one in each subunit of the dimer
-
additional information
-
MtHisD is a bifunctional four-electron dehydrogenase enzyme that catalyzes two subsequent reactions, the oxidation of L-Hol and the reduction of two NAD+ molecules,23 with the formation of two intermediaries, L-histidinaldehyde and L-histidindiol. L-histidinaldehyde is very unstable at neutral pH when not bound to HisD
-
additional information
-
two identical active sites, one in each subunit of the dimer, molecular homology modeling
-
additional information
-
molecular homology model building, overview. His336 plays a critical role in both catalysis and L-Hol binding to MtHisD, Tyr129, Tyr223 and His335 residues make contacts with the substrates in the MtHisD enzyme active site, three-dimensional model analysis, overview
-
additional information
-
two identical active sites, one in each subunit of the dimer
-
additional information
-
residues Glu326 and His327 are directly involved in catalysis, the first participating in acid-base catalysis and the second activating a water molecule, active site structure, overview
-
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Grubmeyer, C.; Teng, H.
Mechanism of Salmonella typhimurium histidinol dehydrogenase: kinetic isotope effects and pH profiles
Biochemistry
38
7355-7362
1999
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Kanaori, K.; Ohta, D.; Nosaka, A.Y.
Effect of excess cadmium ion on the metal binding site of cabbage histidinol dehydrogenase studie by 113Cd-NMR spectroscopy
FEBS Lett.
412
301-304
1997
Brassica oleracea
brenda
Kheirolomoom, A.; Mano, J.; Nagai, A.; Ogawa, A.; Iwasaki, G.; Ohta, D.
Steady-state kinetics of cabbage histidinol dehydrogenase
Arch. Biochem. Biophys.
312
493-500
1994
Brassica oleracea
brenda
Nagai, A.; Ohta, D.
Histidinol dehydrogenase loses its catalytic function through the mutation of His261-Asn due to its inability to ligate the essential Zn
J. Biochem.
115
22-25
1994
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Nagai, A.; Kheirolomoom, A.; Ohta, D.
Site-directed mutagenesis shows that the conserved cysteine residues of histidinol dehydrogensae are not essential for catalysis
J. Biochem.
114
856-861
1993
Brassica oleracea
brenda
Nagai, A.; Suzuku, K.; Ward, E.; Moyer, M.; Hashimoto, M.; Mano, J.; Ohta, D.; Scheidegger, A.
Overexpression of plant histidinol dehydrogenase using baculovirus expression vector system
Arch. Biochem. Biophys.
295
235-239
1992
Brassica oleracea
brenda
Nagai, A.; Ward, E.; Beck, J.; Tada, S.; Chang, J.; Scheidegger, A.
Structural and functional conservation of histidinol dehydrogenase between plants and microbes
Proc. Natl. Acad. Sci. USA
88
4133-4137
1991
Brassica oleracea
brenda
Nagai, A.; Scheidegger, A.
Purification and characterization of histidinol dehydrogenase from cabbage
Arch. Biochem. Biophys.
284
127-132
1991
Asparagus officinalis, Brassica oleracea var. capitata, Brassica oleracea, Cucumis sativus, Lactuca sativa, Rosa sp., Solanum melongena, Triticum aestivum
brenda
Grubmeyer, C.T.; Gray, W.R.
A cysteine residue (cysteine-116) in the histidinol binding site of histidinoldehydrogenase
Biochemistry
25
4778-4784
1986
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Görisch, H.; Hölke, W.
Binding of histidinal to histidinol dehydrogenase
Eur. J. Biochem.
150
305-308
1985
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Andorn, N.; Aronovitch, J.
Purification and properties of histidinol dehydrogenase from Escherichia coli B
J. Gen. Microbiol.
128
579-584
1982
Escherichia coli
brenda
Feingold, D.S.; Franzen, J.S.
Pyridine nucleotide-linked four-electron transfer dehydrogenases
Trends Biochem. Sci.
6
103-105
1981
Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Burger, E.; Görisch, H.
Evidence for an essential lysine at the active site of L-histidinol:NAD+ oxidoreductase; a bifunctional dehydrogenase
Eur. J. Biochem.
118
125-130
1981
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Burger, E.; Görisch, H.; Lingens,
The catalytically active form of histidinol dehydrogenase from Salmonella typhimurium
Biochem. J.
181
771-774
1979
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Bitar, K.G.; Firca, J.R.; Loper, J.C.
Histidinol dehydrogenase from salmonella typhimurium and escherichia coli. Purification, some characteristics and the amino acid sequence around a reactive thiol group
Biochim. Biophys. Acta
493
429-440
1977
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Lindsay, J.A.; Creaser, E.H.
Purification and properties of histidinol dehydrogenases from psychrophilic, mesophilic and thermophilic bacilli
Biochem. J.
165
247-253
1977
Geobacillus stearothermophilus, [Bacillus] caldolyticus, Bacillus subtilis, Sporosarcina psychrophila, Bacillus subtilis HT1
brenda
Yang, H.J.; Lee, B.; Haslam, J.L.
Studies on histidinol dehydrogenase preliminary crystallographic data
J. Mol. Biol.
81
517-519
1973
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Loper, J.C.; Adams, E.
Purification and properties of histidinol dehydrogenase from Salmonella typhimurium
J. Biol. Chem.
240
788-795
1965
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Adams, E.
The enzymatic synthesis of histidine from histidinol
J. Biol. Chem.
209
829-846
1954
Paenarthrobacter histidinolovorans, Escherichia coli
brenda
Wadud, S.; Or-Rashid, M.M.; Onodera, R.
Method for determination of histidine in tissues by isocratic high-performance liquid chromatography and its application to the measurement of histidinol dehydrogenase activity in six cattle organs
J. Chromatogr. B
767
369-374
2002
Bos taurus
brenda
Barbosa, J.A.; Sivaraman, J.; Li, Y.; Larocque, R.; Matte, A.; Schrag, J.D.; Cygler, M.
Mechanism of action and NAD+-binding mode revealed by the crystal structure of L-histidinol dehydrogenase
Proc. Natl. Acad. Sci. USA
99
1859-1864
2002
Escherichia coli (P06988), Escherichia coli
brenda
Joseph, P.; Abdo, M.R.; Boigegrain, R.A.; Montero, J.L.; Winum, J.Y.; Koehler, S.
Targeting of the Brucella suis virulence factor histidinol dehydrogenase by histidinol analogues results in inhibition of intramacrophagic multiplication of the pathogen
Antimicrob. Agents Chemother.
51
3752-3755
2007
Brucella suis
brenda
Abdo, M.R.; Joseph, P.; Boigegrain, R.A.; Montero, J.L.; Kohler, S.; Winum, J.Y.
Brucella suis histidinol dehydrogenase: Synthesis and inhibition studies of substituted N-L-histidinylphenylsulfonyl hydrazide
J. Enzyme Inhib. Med. Chem.
23
357-361
2008
Brucella suis
brenda
Pahwa, S.; Chavan, A.G.; Jain, R.; Roy, N.
Target-specific anti-fungal discovery by targeting Geotrichum candidum histidinol dehydrogenase: a hybrid approach
Chem. Biol. Drug Des.
72
229-234
2008
Geotrichum candidum
brenda
Pahwa, S.; Kaur, S.; Jain, R.; Roy, N.
Structure based design of novel inhibitors for histidinol dehydrogenase from Geotrichum candidum
Bioorg. Med. Chem. Lett.
20
3972-3976
2010
Geotrichum candidum (A1BPP9), Geotrichum candidum
brenda
Nunes, J.E.; Ducati, R.G.; Breda, A.; Rosado, L.A.; de Souza, B.M.; Palma, M.S.; Santos, D.S.; Basso, L.A.
Molecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23)
Arch. Biochem. Biophys.
512
143-153
2011
Mycobacterium tuberculosis (P9WNW9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WNW9)
brenda
Turtaut, F.; Ouahrani-Bettache, S.; Montero, J.; Köhler, S.; Winum, J.
Synthesis and biological evaluation of a new class of anti-brucella compounds targeting histidinol dehydrogenase: alpha-O-arylketones and alpha-S-arylketones derived from histidine
MedChemComm
2
995-1000
2011
Brucella sp.
-
brenda
Abdo, M.R.; Joseph, P.; Mortier, J.; Turtaut, F.; Montero, J.L.; Masereel, B.; Koehler, S.; Winum, J.Y.
Anti-virulence strategy against Brucella suis: synthesis, biological evaluation and molecular modeling of selective histidinol dehydrogenase inhibitors
Org. Biomol. Chem.
9
3681-3690
2011
Brucella suis
brenda
D'Ambrosio, K.; Lopez, M.; Dathan, N.A.; Ouahrani-Bettache, S.; Koehler, S.; Ascione, G.; Monti, S.M.; Winum, J.Y.; De Simone, G.
Structural basis for the rational design of new anti-Brucella agents: the crystal structure of the C366S mutant of L-histidinol dehydrogenase from Brucella suis
Biochimie
97
114-120
2014
Brucella suis bv. 1 (Q8G2R2), Brucella suis bv. 1 1330 (Q8G2R2)
brenda
Turtaut, F.; Lopez, M.; Ouahrani-Bettache, S.; Koehler, S.; Winum, J.Y.
Oxo- and thiooxo-imidazo[1,5-c]pyrimidine molecule library: beyond their interest in inhibition of Brucella suis histidinol dehydrogenase, a powerful protection tool in the synthesis of histidine analogues
Bioorg. Med. Chem. Lett.
24
5008-5010
2014
Brucella suis
brenda
Lunardi, J.; Borges Martinelli, L.; Raupp, A.; Sacconi Nunes, J.; Rostirolla, D.; Saraiva Macdo Timmers, L.; Villela, A.; Pissinate, K.; Limberger, J.; Norberto De Souza, O.; Basso, L.; Santos, D.; Machado, P.
Mycobacterium tuberculosis histidinol dehydrogenase: Biochemical characterization and inhibition studies
RSC Adv.
6
28406-28418
2016
Mycobacterium tuberculosis (P9WNW9), Mycobacterium tuberculosis H37Rv (P9WNW9)
-
brenda
Koehler, S.; Dessolin, J.; Winum, J.
Inhibitors of histidinol dehydrogenase
Top. Med. Chem.
22
35-46
2017
Brucella sp., Geotrichum candidum (A0A0J9X7D2), Escherichia coli (P06988), Salmonella enterica subsp. enterica serovar Typhimurium (P10370), Brassica oleracea (P24226), Mycobacterium tuberculosis (P9WNW9), Burkholderia pseudomallei (Q63Q86), Brucella suis (Q8G2R2), Brucella suis 1330 (Q8G2R2), Mycobacterium tuberculosis H37Rv (P9WNW9), Burkholderia pseudomallei K96243 (Q63Q86)
-
brenda
Ruszkowski, M.; Dauter, Z.
Structures of Medicago truncatula L-histidinol dehydrogenase show rearrangements required for NAD+ binding and the cofactor positioned to accept a hydride
Sci. Rep.
7
10476
2017
Medicago truncatula (G7IKX3), Medicago truncatula
brenda