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Literature summary for 1.4.3.16 extracted from

  • Chow, C.; Hegde, S.; Blanchard, J.S.
    Mechanistic characterization of Escherichia coli L-aspartate oxidase from kinetic isotope effects (2017), Biochemistry, 56, 4044-4052 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.16

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli BL21(DE3) Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate + O2 Escherichia coli the first enzyme in the de novo synthesis of NAD+ in bacteria iminosuccinate + H2O2
-
 ?
L-aspartate + O2 Escherichia coli K12 the first enzyme in the de novo synthesis of NAD+ in bacteria iminosuccinate + H2O2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli K12
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate + H2O + fumarate can use either molecular oxygen or fumarate to reoxidize the reduced enzyme Escherichia coli oxaloacetate + NH3 + succinate
-
 ?
L-aspartate + H2O + fumarate can use either molecular oxygen or fumarate to reoxidize the reduced enzyme Escherichia coli K12 oxaloacetate + NH3 + succinate
-
 ?
L-aspartate + O2 the first enzyme in the de novo synthesis of NAD+ in bacteria Escherichia coli iminosuccinate + H2O2
-
 ?
L-aspartate + O2 can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. The chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of L-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the alpha-amine Escherichia coli iminosuccinate + H2O2
-
 ?
L-aspartate + O2 the first enzyme in the de novo synthesis of NAD+ in bacteria Escherichia coli K12 iminosuccinate + H2O2
-
 ?
L-aspartate + O2 can use either molecular oxygen or fumarate to reoxidize the reduced enzyme. The chemistry is similar to that of typical amino acid oxidases in which the transfer of the hydride from C2 of L-aspartate to FAD is rate-limiting and occurs in a concerted manner with respect to deprotonation of the alpha-amine Escherichia coli K12 iminosuccinate + H2O2
-
 ?

Synonyms

Synonyms Comment Organism
L-aspartate oxidase
-
 Escherichia coli
nadB
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD FAD-dependent enzyme Escherichia coli

General Information

General Information Comment Organism
evolution NadB has structurally evolved from succinate dehydrogenase/fumarate reductase-type enzymes to gain the new functionality of oxidizing amino acids while retaining the ability to reduce fumarate Escherichia coli
metabolism the first enzyme in the de novo synthesis of NAD+ in bacteria Escherichia coli