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17-(3-carboxypropyl)-5,10,15,20,22,24-hexahydro-3,7,13,18-tetramethyl-21H,23H-porphine-2,8,12-tripropanoic acid + O2
? + CO2
-
generates a vinyl group on ring-A
-
?
17-ethyl harderoporphyrinogen-III + O2 + 2 H+
?
-
-
-
-
?
17-ethylharderoporphyrinogen-III + O2 + 2 H+
17-ethylprotoporphyrinogen-IX + 2 CO2 + 2 H2O
2,4-bis-(beta-hydroxypropionic acid) deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
-
one sixth of the rate compared to coproporhyrinogen-III
-
?
2-beta-hydroxypropionic acid-4-propionic acid deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
-
80% of the activity compared to coproporphyrinogen-III
-
?
2-propionic acid-4-beta-hydroxypropionic acid deuteroporphyrinogen IX + O2
protoporphyrinogen IX + CO2
-
8% of the activity compared to coproporphyrinogen-III
-
?
3-[7,13-di(2-carboxy-ethyl)-17-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13-(2-carboxy-ethyl)-17-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
?
3-[7,13-di(2-carboxy-ethyl)-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13-(2-carboxy-ethyl)-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + 3-[7,13-divinyl-17-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7,17-di(2-carboxy-ethyl)-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-17-(2-carboxy-ethyl)-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
?
3-[7,17-di(2-carboxy-ethyl)-13-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-17-(2-carboxy-ethyl)-13-ethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-di-tert-butyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-di-tert-butyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-dibutyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-dibutyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
3-[7-(2-carboxy-ethyl)-13,17-diisopropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-diisopropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-dipropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-dipropyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
3-[7-(2-carboxy-ethyl)-3,8,12,13,17,18-hexamethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-3,8,12,13,17,18-hexamethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
?
3-[7-(2-carboxy-ethyl)-3,8,12,13,17,18-hexamethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-3,8,12,13,17,18-hexamethyl-porphyrinogen-2-yl]-propionic acid + CO2 + CO2
-
-
-
-
?
3-[7-vinyl-17-(2-carboxy-ethyl)-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[2,7-divinyl-13-benzyl-3,8,12,18-tetramethyl-porphyrinogen-17-yl]-propionic acid + CO2
-
-
-
?
4,4'-[7,12-bis(2-carboxyethyl)-3,8,13,17-tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,18-diyl]dibutanoic acid + O2 + 2 H+
? + 2 CO2 + 2 H2O
5,10,15,20,22,24-hexahydro-3,7,13,18-tetramethyl-21H,23H-porphine-2,8,12,17-tripropanoic acid 17-methyl ester + O2
? + CO2
-
very poor substrate
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
coproporphyrinogen-III + O2 + 2 H+
harderoporphyrinogen + CO2 + 2 H2O
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
coproporphyrinogen-III + O2 + 2H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
coproporphyrinogen-IV + O2
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen + CO2 + H2O
substrate undergoes only the second decarboxylation
-
-
?
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen-IX + CO2 + 2 H2O
harderoporphyrinogen + O2 + H+
protoporphyrinogen IX + CO2 + H2O2
harderoporphyrinogen-III + O2 + 2 H+
?
-
-
-
-
?
harderoporphyrinogen-IV + O2 + 2 H+
?
-
-
-
-
?
harderoporphyrinogen-VII + O2 + 2 H+
?
-
a monovinyl intermediate in the metabolism of coproporphyrinogen-IV
-
-
?
harderoporphyrinogen-VII + O2 + 2 H+
? + 2 CO2 + 2 H2O
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
isoharderoporphyrinogen + O2 + 2 H+
?
-
very low activity
-
-
?
isoharderoporphyrinogen + O2 + 2 H+
? + 2 CO2 + 2 H2O
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
mesoporphyrinogen-VI + O2 + H+
? + CO2 + H2O
substrate undergoes only the first oxidative decarboxylation
-
-
?
mesoproporphyrinogen-VI + O2
?
pentacarboxylate porphyrinogen 5dab + O2
dehydroisocoproporphyrinogen
-
poorer substrate than coproporphyrinogen-III
-
-
?
pentacarboxylate porphyrinogen III + O2
dehydroisocoproporphyrinogen + CO2
-
half of the activity compared to coproporphyrinogen oxidase-III
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen-IX + O2
protoporphyrin IX + CO2
-
capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
-
?
protoporphyrinogen-IX + O2
protoporphyrin-IX + CO2
-
capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
-
?
additional information
?
-
17-ethylharderoporphyrinogen-III + O2 + 2 H+
17-ethylprotoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
17-ethylharderoporphyrinogen-III + O2 + 2 H+
17-ethylprotoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
?
3-[7-(2-carboxy-ethyl)-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + O2
3-[7-vinyl-13,17-diethyl-3,8,12,18-tetramethyl-porphyrinogen-2-yl]-propionic acid + CO2
-
-
-
-
?
4,4'-[7,12-bis(2-carboxyethyl)-3,8,13,17-tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,18-diyl]dibutanoic acid + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
-
major product is a monovinylporphyrinogen, but some divinyl product is also generated. The incubation products are converted into the corresponding porphyrin methyl esters, and characterized by proton NMR spectroscopy and mass spectrometry
-
?
4,4'-[7,12-bis(2-carboxyethyl)-3,8,13,17-tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,18-diyl]dibutanoic acid + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
-
major product is a monovinylporphyrinogen, but some divinyl products are also generated. The incubation products are converted into the corresponding porphyrin methyl esters, and characterized by proton NMR spectroscopy and mass spectrometry
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
recombinant Sll1185 shows CPO activity under both aerobic and anaerobic conditions
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
two oxidative decarboxylations sequentially to give a monovinylporphyrinogen intermediate. Regiospecific generation of harderoporphyrinogen as an intermediate by first converting the A ring side chain to a vinyl unit. Type isomers of coproporphyrinogen, overview
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
via harderoporphyrinogen intermediate production, overall reaction
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
two oxidative decarboxylations sequentially to give a monovinylporphyrinogen intermediate Regiospecific generation of harderoporphyrinogen as an intermediate by first converting the A ring side chain to a vinyl unit. Type isomers of coproporphyrinogen, overview
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
-
-
-
?
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
-
-
-
?
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
-
oxidation under anaerobic conditions strictly requires NADP+ as electron acceptor
-
?
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
-
oxidation under anaerobic conditions strictly requires NADP+ as electron acceptor
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic oxidation only in the presence of ATP, NADP+, Mg2+, L-Met, 5-10% of the aerobic activity
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
Chromatium sp.
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
-
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
essential enzyme, catalyzes the 6th step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
O2-dependent enzyme Hem13p
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
enzyme is involved in heme and chlorophyll biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
HemF is absolutely dependent on oxygen
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
pathway overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
coproporphyrinogen analogues with modified propionate side chains bearing methyl substitutents are moderate substrates for the enzyme giving divinylic products, overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
pathway overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
6th step in heme biosynthesis, pathway overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
key enzyme in the biosynthesis of heme, metabolism overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
conversion of 2 propionate groups to 2 vinyl groups by oxidative decarboxylation
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
coproporphyrinogen conversion via tripropionate intermediate harderoporphyrinogen, selective conversion of propionate residues at the A and B rings into vinyl moieties by oxidation and decarboxylation resulting in a trivinylic compound
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
sequential oxidative decarboxylations at the A and B rings, synthetic coproporphyrinogen analogues with modified methylated propionate side chains are moderate substrates for the enzyme giving divinylic products, overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
-
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
enzyme is involved in heme and chlorophyll biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
-
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
6th step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
enzyme catalyzes the 6th step in heme biosynthesis, heme might be a feed-back regulator of its synthesis by inhibiting the import of th enzyme into mitochondria
-
-
?
coproporphyrinogen-III + O2 + 2 H+
harderoporphyrinogen + CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
harderoporphyrinogen + CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
highly specific for oxygen as electron acceptor
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Chromatium sp.
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Chromatium sp.
-
highly specific for oxygen as electron acceptor
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
highly specific for oxygen as electron acceptor
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
oxygen-independent enzyme has also an aerobic function
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
acts on analogues which possess normal substituents on ring-A to generate a vinyl group on that ring, not active if the ring-A propionate group is changed
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Arg400, Arg262 and Arg401 are active amino acids critical for substrate binding and/or catalysis, Arg262 and 401 may coordinate carboxylate groups of coproporphyrinogen-III, while Asp400 may initiate deprotonation of substrate, resulting in oxidative decarboxylation
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
small amount of the monovinyl intermediate
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
CPO converts coproporphyrinogen III to protoporphyrinogen IX through harderoporphyrinogen IX
-
-
ir
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
O2 is added to the (preferentially deprotonated) pyrrole substrate (yielding a hydroperoxide, which then abstracts a proton from the reactive propionate substituent), the reaction may then proceed through HO2- elimination, followed by decarboxylation
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
sixths enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
sixths enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
6th enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
6th enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
step-wise decarboxylation of 2- and 4-propionate substituents, both decarboxylations take place at the same active centre
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
highly specific for oxygen as electron acceptor
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
sixths enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
6th enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
same activity under aerobic and anaerobic conditions
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
aerobic and anaerobic oxidation catalyzed by the same enzyme
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
sixths enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
6th enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen-III + O2 + 2H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
CPO catalyzes the conversion of coproporphyrinogen-III to protoporphyrinogen-IX, a divinyl product, via two sequential oxidative decarboxylations of the A and B ring propionates
-
-
?
coproporphyrinogen-IV + O2
?
-
synthetic coproporphyrinogen analogues with modified propionate side chains
-
-
?
coproporphyrinogen-IV + O2
?
-
synthetic coproporphyrinogen analogues with modified propionate side chains
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
monovinyl intermediate that accumulates before being converted to an isomer
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
-
-
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
30% higher activity compared to coproporphyrinogen-III
-
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
-
-
-
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
-
-
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
-
-
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
intermediate of coproporphyrinogen-III, that is also a substrate
-
?
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen-IX + CO2 + 2 H2O
-
-
-
?
harderoporphyrinogen + O2 + 2 H+
protoporphyrinogen-IX + CO2 + 2 H2O
-
-
-
?
harderoporphyrinogen + O2 + H+
protoporphyrinogen IX + CO2 + H2O2
-
-
-
r
harderoporphyrinogen + O2 + H+
protoporphyrinogen IX + CO2 + H2O2
-
-
-
-
r
harderoporphyrinogen-VII + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
-
-
-
?
harderoporphyrinogen-VII + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
-
-
-
?
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
3% of the activity compared to coproporphyrinogen-III
-
?
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
intermediate of coproporphyrinogen-III that is also a substrate
-
?
isoharderoporphyrinogen + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
-
-
-
?
isoharderoporphyrinogen + O2 + 2 H+
? + 2 CO2 + 2 H2O
-
-
-
-
?
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
-
similar oxidation rate compared to coproporphyrinogen-III
-
?
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
-
-
-
?
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
-
-
-
r
mesoproporphyrinogen-VI + O2
?
-
synthetic coproporphyrinogen analogues with modified propionate side chains
-
-
?
mesoproporphyrinogen-VI + O2
?
-
synthetic coproporphyrinogen analogues with modified propionate side chains
-
-
?
additional information
?
-
-
no activity of HemF with protoporphyrinogen-IX and coporphyrinogen-III
-
-
?
additional information
?
-
-
substrate specificity with diverse coproporphyrinogen-derived compounds, overview, alterations of substituents involved in secondary binding interactions have a comparable affect to modifying the side chain that undergoes degradation at the catalytic site, porphyrinogen carboxylic acids are unstable, no hyroxylated products
-
-
?
additional information
?
-
-
substrate specificity with diverse coproporphyrinogen-derived compounds, overview, alterations of substituents involved in secondary binding interactions have a comparable affect to modifying the side chain that undergoes degradation at the catalytic site, no hyroxylated products
-
-
?
additional information
?
-
-
a nonnatural type I isomer of harderoporphyrinogen is also a substrate of CPO, no activity with 13-ethyl harderoporphyrinogen-III, substrate specificity with vinylic porphyrinogen derivatives, harderoporphyrinogen derivatives, and reaction mechanism, detailed overview
-
-
?
additional information
?
-
-
porphyrinogen 3,3'-[13,17-bis(carboxymethyl)-3,8,12,18-tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,7-diyl]dipropanoic acid proves to be a relatively poor substrate for CPO compared to the natural substrate coproporphyrinogen-III, and only the A ring propionate moiety is processed to a significant extent
-
-
?
additional information
?
-
-
pentacarboxylate porphyrinogens 5abc, 5abd, and 5acd are not metabolized
-
-
?
additional information
?
-
-
porphyrinogen 3,3'-[13,17-bis(carboxymethyl)-3,8,12,18-tetramethyl-5,10,15,20,22,24-hexahydroporphyrin-2,7-diyl]dipropanoic acid proves to be a relatively poor substrate for CPO compared to the natural substrate coproporphyrinogen-III, and only the A ring propionate moiety is processed to a significant extent. Substrate recognition and catalysis, overview
-
-
?
additional information
?
-
-
the 17-ethyl analogue of harderoporphyrinogen-III, but not its 13-ethyl isomer, is an excellent substrate for the enzyme in accord with a proposed model for the active site of the enzyme. Harderoporphyrinogen-VII, the monovinyl intermediate in the metabolism of coproporphyrinogen-IV, is an equally good substrate
-
-
?
additional information
?
-
-
no activity with S-adenosylmethionine or without O2
-
-
?
additional information
?
-
-
deleterious enzyme mutations can cause hereditary coproporphyria
-
-
?
additional information
?
-
-
the 17-ethyl analogue of harderoporphyrinogen-III, but not its 13-ethyl isomer, is an excellent substrate for the enzyme in accord with a proposed model for the active site of the enzyme. Harderoporphyrinogen-VII, the monovinyl intermediate in the metabolism of coproporphyrinogen-IV, is an equally good substrate
-
-
?
additional information
?
-
no anaerobic activity is detected using NADP+ and S-adenosylmethionine
-
-
?
additional information
?
-
-
no anaerobic activity is detected using NADP+ and S-adenosylmethionine
-
-
?
additional information
?
-
-
HemJ is functionally coupled with the enzyme
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
coproporphyrinogen III + O2
coproporphyrin III + H2O
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
essential enzyme, catalyzes the 6th step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
mesoporphyrinogen-VI + O2 + 2 H+
protoaetioporphyrin + 2 CO2 + 2 H2O
-
similar oxidation rate compared to coproporphyrinogen-III
-
?
pentacarboxylate porphyrinogen III + O2
dehydroisocoproporphyrinogen + CO2
-
half of the activity compared to coproporphyrinogen oxidase-III
-
?
protoporphyrinogen IX + O2
protoporphyrin IX + H2O
-
-
-
-
?
protoporphyrinogen-IX + O2
protoporphyrin-IX + CO2
-
capacity to oxidize not only coproporphyrinogen-III but also protoporphyrinogen-IX
-
?
additional information
?
-
-
deleterious enzyme mutations can cause hereditary coproporphyria
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
-
?
coproporphyrinogen III + O2
coproporphyrin III + H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
via harderoporphyrinogen intermediate production, overall reaction
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
-
?
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
-
-
-
?
coproporphyrinogen III + O2 + H+
protoporphyrinogen IX + CO2 + H2O
-
-
-
?
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
-
oxidation under anaerobic conditions strictly requires NADP+ as electron acceptor
-
?
coproporphyrinogen-III + 2 NADP+
protoporphyrinogen-IX + 2 CO2 + 2 NADPH + 2 H+
-
oxidation under anaerobic conditions strictly requires NADP+ as electron acceptor
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic oxidation only in the presence of ATP, NADP+, Mg2+, L-Met, 5-10% of the aerobic activity
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
Chromatium sp.
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
?
coproporphyrinogen-III + ?
protoporphyrinogen-IX + ?
-
anaerobic enzyme, presence of Mg2+, L-Met, ATP, NADH and NADP+
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
enzyme is involved in heme and chlorophyll biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
pathway overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
pathway overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
6th step in heme biosynthesis, pathway overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
key enzyme in the biosynthesis of heme, metabolism overview
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
enzyme is involved in heme and chlorophyll biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
6th step in heme biosynthesis
-
-
?
coproporphyrinogen-III + O2
protoporphyrinogen-IX + CO2 + H2O
-
enzyme catalyzes the 6th step in heme biosynthesis, heme might be a feed-back regulator of its synthesis by inhibiting the import of th enzyme into mitochondria
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
highly specific for oxygen as electron acceptor
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Chromatium sp.
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
Chromatium sp.
-
highly specific for oxygen as electron acceptor
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
highly specific for oxygen as electron acceptor
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
oxygen-independent enzyme has also an aerobic function
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
acts on analogues which possess normal substituents on ring-A to generate a vinyl group on that ring, not active if the ring-A propionate group is changed
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
6th enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
6th enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
step-wise decarboxylation of 2- and 4-propionate substituents, both decarboxylations take place at the same active centre
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
highly specific for oxygen as electron acceptor
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
6th enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
same activity under aerobic and anaerobic conditions
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
aerobic and anaerobic oxidation catalyzed by the same enzyme
-
?
coproporphyrinogen-III + O2 + 2 H+
protoporphyrinogen-IX + 2 CO2 + 2 H2O
-
6th enzyme in heme biosynthetic pathway
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
-
-
?
coproporphyrinogen-IV + O2
protoporphyrinogen-XIII + 2 CO2 + 2 H2O
-
-
-
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
30% higher activity compared to coproporphyrinogen-III
-
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
-
-
?
harderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
intermediate of coproporphyrinogen-III, that is also a substrate
-
?
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
3% of the activity compared to coproporphyrinogen-III
-
?
isoharderoporphyrinogen + O2
protoporphyrinogen IX + CO2 + H2O2
-
intermediate of coproporphyrinogen-III that is also a substrate
-
?
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C167S
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
G127V
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
H106L
-
site-directed mutagenesis, inactive mutant
H145L
-
site-directed mutagenesis, inactive mutant
H175L
-
site-directed mutagenesis, inactive mutant
H96L
-
site-directed mutagenesis, inactive mutant
P133A
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
T132A
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W123L
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W124R
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W166L
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W274L
-
site-directed mutagenesis, inactive mutant
W298L
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
W36L
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y135F
-
site-directed mutagenesis, activity similar to the wild-type
Y160F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y170F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y213F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y240F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
Y276F
-
site-directed mutagenesis, activity and kinetics similar to the wild-type
A174T
the mutation is associated with hepatic porphyrias
A203T
-
natural mutation due to single nucleotide substitution 607G>A, identified in a patient with hereditary coproporphyria
C357T
the mutation is associated with hepatic porphyrias
C991T/C1339T
-
identification of 2 coexisting mutations, C991T and C1339T, on a single allele in the enzyme' gene in Swedish patients with hereditary coproporphyria, biochemical analysis of the patients carrying the mutations, overview
D233G/DELTA403-406
-
the mutations are associated with harderoporphyria
D400R
-
less than 1% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
delL311/delY312
the mutation is associated with hepatic porphyrias
F395G
-
4% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
F405G
-
1% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
G188W
-
a naturally occuring frameshift mutation p.Gly188TrpfsX45 in hereditary coproporphyria patient from Italian population, phenotype, overview
G279R
novel nucleotide transition found, is unstable, and produces ca. 2-5% of activity compared with the wild-type CPO
G402A
-
less than 1% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
G402D
site-directed mutagenesis, the mutant enzyme forms dimers
G65S
the mutation is associated with hepatic porphyrias
Gln221GlufsX10
the mutation is associated with hepatic porphyrias
H148A
retains 39% of wild type enzyme activity for the overall conversion of coproporphyrinogen-III to protoporphyrinogen-IX
H158A
the mutant exhibits approximately 50fold lower activity than wild type recombinant CPO for the conversion of coproporphyrinogen-III to protoporphyrinogen-IX
H197A
the mutant exhibits approximately 50fold lower activity for the overall conversion of coproporphyrinogen-III to protoporphyrinogen-IX than wild type recombinant CPO, but the second oxidative decarboxylation step is not impaired, with mutant enzyme H197A retaining 100% of the wild type activity using harderoporphyrinogen as substrate
H227A
catalyzes the conversion of coproporphyrinogen-III to protoporphyrinogen-IX at a rate almost 2fold that of the wild type enzyme
H327RE
-
the mutation is associated with harderoporphyria
K404H
site-directed mutagenesis, the mutant produces a high level of harderoporphyrinogen with low production of protoporphyrinogen similar to mutant K404E
K404N
-
61% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
K404Q
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
L288W
-
the mutation is associated with hereditary coproporphyria with posterior reversible encephalopathy
L35H
the mutation is associated with hepatic porphyrias
N272H
-
natural polymorphism, twofold decrease in affinity for coproporphyrinogen-III. Specific activity in liver samples is 40-50% lower than in wild-type
R231W
-
lowers Vmax-value, 4 fold lower catalytic efficiency
R262G
the mutation is associated with hepatic porphyrias
R332W
the mutation is associated with hepatic porphyrias
R388W
site-directed mutagenesis, the mutant enzyme forms dimers
R391W
site-directed mutagenesis, the mutant enzyme forms dimers
R401D
-
45% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
R401K
-
63% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
T403N
-
31% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
V16G
the mutation is associated with hepatic porphyrias
V209D
the mutation is associated with hepatic porphyrias
W73C
the mutation is associated with hepatic porphyrias
Y399L
-
81% of residual activity compared with wild-type CPO, shows accumulation of coproporphyrinogen
H158A
-
complete loss of activity, decreased stability, no copper content
D274A
-
site-directed mutagensis, inactive mutant
H131A
-
site-directed mutagensis, inactive mutant
R135A
-
site-directed mutagensis, inactive mutant
R275A
-
site-directed mutagensis, inactive mutant
D400A
impaired catalytic ability, with 0.047% of wild-type total product efficiency
D400A
the mutant produces no divinyl product, the Km value for coproporphyrinogen-III does not change significantly compared to the wild-type enzyme
D400A
the mutation impairs the catalytic ability of CPO relative to the wild type enzyme, not able to form divinyl products, but the Km value for coproporphyrinogen-III does not change significantly compared to the wild-type enzyme
D400A
site-directed mutagenesis, the inactive mutant D400A remains in a monomeric form
D400A
mutation severely impaires the catalytic activity, mutant performs, on average, less than a single turnover
G242C
-
natural mutation due to single nucleotide substitution 724G>T, identified in a patient with hereditary coproporphyria
G242C
-
a naturally occuring missense mutation in hereditary coproporphyria patient from Italian population, phenotype, overview
K404E
-
66% of residual activity compared with wild-type CPO, causes substantial accumulation of harderoporphyrinogen
K404E
a naturally occuring mutant derived from patients with harderoporphyria, the mutant produces less harderoporphyrinogen. The K404E mutation leads to diminishment of the second step of the decarboxylation reaction during the conversion of coproporphyrinogen to protoporphyrinogen. The mutant enzyme forms dimers
K404E
-
the mutation is associated with harderoporphyria
L398P
-
natural mutation due to single nucleotide substitution 1193T>C, identified in a patient with hereditary coproporphyria
L398P
-
a naturally occuring missense mutation in hereditary coproporphyria patient from Italian population, phenotype, overview
R262A
impaired catalytic ability, with 0.00036% of wild-type total product efficiency
R262A
poor catalyst for the production of a divinyl product with a catalytic efficiency less than 0.01% compared to wild-type, including a 15fold higher Km for coproporphyrinogen-III
R262A
the mutant CPO is a poor catalyst for the production of a divinyl product, with a catalytic efficiency less than 0.01% compared to the wild type enzyme including a 15fold higher Km for coproporphyrinogen-III
R262A
mutation results in decreased kcat values and increased Km values. No product formation is detected with sunstrate mesoporphyrogen-VI
R401A
impaired catalytic ability, with 44% of wild-type total product efficiency
R401A
the efficiency of divinyl product formation for mutant enzyme R401A is about 3% compared to wild type CPO, with a 3fold increase in the Km value for coproporphyrinogen-III
R401A
the efficiency of divinyl product formation is about 3% compared to the wild type enzyme
R401A
mutation results in decreased kcat values and increased Km values. The mutant is able to convert mesoporphyrogen-VI to monovinyl product, although over 10fold less efficiently than wild-type
R401W
-
75% of residual activity compared with wild-type CPO, causes substantial accumulation of harderoporphyrinogen
R401W
site-directed mutagenesis, the mutant enzyme forms dimers
S245F
-
natural mutation due to single nucleotide substitution 734C>T, identified in a patient with hereditary coproporphyria
S245F
-
a naturally occuring missense mutation in hereditary coproporphyria patient from Italian population, phenotype, overview
additional information
spontaneous lesion formation mutant lin2-2
additional information
-
spontaneous lesion formation mutant lin2-2
-
additional information
construction of a hemF and hemH deletion plasmids by transforming the linearized disruption vectors pDELTAhemF and pDELTAhemH into strain AB4.1, strain N402 genomic DNA is used as a template. Deletion of hemF (CPO) or hemH (FC) is conditionally lethal, and despite supplementation of hemin, DELTAhemF and DELTAhemH strains are still extremely impaired in growth. Co-overexpression of hemH, hemF, and the aminolevulinic acid synthase encoding hemA, increases the cellular accumulation of porphyrin intermediates suggesting regulatory mechanisms operating in the final steps of the fungal heme biosynthesis pathway. Gene hemF deletion strain displays a specific pigmented phenotype due to coproporphyrinogen III accumulation. Phenotypes, overview
additional information
-
construction of a hemF and hemH deletion plasmids by transforming the linearized disruption vectors pDELTAhemF and pDELTAhemH into strain AB4.1, strain N402 genomic DNA is used as a template. Deletion of hemF (CPO) or hemH (FC) is conditionally lethal, and despite supplementation of hemin, DELTAhemF and DELTAhemH strains are still extremely impaired in growth. Co-overexpression of hemH, hemF, and the aminolevulinic acid synthase encoding hemA, increases the cellular accumulation of porphyrin intermediates suggesting regulatory mechanisms operating in the final steps of the fungal heme biosynthesis pathway. Gene hemF deletion strain displays a specific pigmented phenotype due to coproporphyrinogen III accumulation. Phenotypes, overview
additional information
-
construction of a hemF and hemH deletion plasmids by transforming the linearized disruption vectors pDELTAhemF and pDELTAhemH into strain AB4.1, strain N402 genomic DNA is used as a template. Deletion of hemF (CPO) or hemH (FC) is conditionally lethal, and despite supplementation of hemin, DELTAhemF and DELTAhemH strains are still extremely impaired in growth. Co-overexpression of hemH, hemF, and the aminolevulinic acid synthase encoding hemA, increases the cellular accumulation of porphyrin intermediates suggesting regulatory mechanisms operating in the final steps of the fungal heme biosynthesis pathway. Gene hemF deletion strain displays a specific pigmented phenotype due to coproporphyrinogen III accumulation. Phenotypes, overview
-
additional information
-
HemF- mutant strain, unable to grow under aerobic condition
additional information
-
18-somite stage cloche homozygous mutant embryos, development of hematopoietic and endothelial lineages is severely impaired, cpo is downregulated
additional information
-
knockdown of zebrafish CPO using anti-sense morpholinos leads to a significant suppression of hemoglobin production without apparent reduction of blood cells, injection of human CPO RNA, but not a mutant CPO RNA similar to a mutant responsible for a hereditary coproporphyria, restores hemoglobin production in the CPO-MO-injected embryos, expression of CPO in the ICM is severely suppressed in both vlad tepes/gata1 mutants and in biklf-MO-injected embryos
additional information
-
mutation of the nucleotide binding motif GGGXXTP does not affect the enzyme activity
additional information
-
a duplication of a T in position 561 of the coding sequence, i.e.561dupT in exon 2 results in a frameshift that gives rise to a stop codon 45 residues downstream Glycine at position 188, i.e. p.Gly188TrpfsX45. Mutation identified in a patient with hereditary coproporphyria
additional information
enzyme engineering of mutant homodimer and heterodimer of coproporphyinogen oxidase. The His-tagged mutant enzyme forms a heterodimer in association with the HA-tagged wild-type enzyme, The monomeric form of mutated CPOX does not show any activity and homodimeric enzymes derived from hereditary coproporphyria (HCP) mutant show low activity (about 20% of the control). The chimeric heterodimers with wild-type and mutated subunits from HCP patients show low protoporphyrinogen producing activity. Some mutations of amino acids 401-404 are associated with marked accumulation of reaction intermediate harderoporphyrinogen, with a decrease in the production of protoporphyrinogen, whereas K404E derived from patients with harderoporphyria produces less harderoporphyrinogen. Functional analysis of heterodimer of mutant/wild-type complex, heterophilic forms of His-R388W/HA-wild-type, His-R391W/HA-wild-type, His-D400A/HA-wild-type, His-R401W/HA-wild-type, His-G402D/HA-wild-type and His-K404E/HA-wild-type, overview
additional information
-
enzyme engineering of mutant homodimer and heterodimer of coproporphyinogen oxidase. The His-tagged mutant enzyme forms a heterodimer in association with the HA-tagged wild-type enzyme, The monomeric form of mutated CPOX does not show any activity and homodimeric enzymes derived from hereditary coproporphyria (HCP) mutant show low activity (about 20% of the control). The chimeric heterodimers with wild-type and mutated subunits from HCP patients show low protoporphyrinogen producing activity. Some mutations of amino acids 401-404 are associated with marked accumulation of reaction intermediate harderoporphyrinogen, with a decrease in the production of protoporphyrinogen, whereas K404E derived from patients with harderoporphyria produces less harderoporphyrinogen. Functional analysis of heterodimer of mutant/wild-type complex, heterophilic forms of His-R388W/HA-wild-type, His-R391W/HA-wild-type, His-D400A/HA-wild-type, His-R401W/HA-wild-type, His-G402D/HA-wild-type and His-K404E/HA-wild-type, overview
additional information
loss of inducibility due to the promoter mutations occur reproducibly with all C/EBP isoforms, arguing that CPO promoter activity depends upon C/EBP site location, and not simply upon inherent binding affinity, hypothetical modeling, overview
additional information
loss of inducibility due to the promoter mutations occur reproducibly with all C/EBP isoforms, arguing that CPO promoter activity depends upon C/EBP site location, and not simply upon inherent binding affinity, hypothetical modeling, overview
additional information
-
loss of inducibility due to the promoter mutations occur reproducibly with all C/EBP isoforms, arguing that CPO promoter activity depends upon C/EBP site location, and not simply upon inherent binding affinity, hypothetical modeling, overview
additional information
-
identification of diverse deleterious enzyme mutations in hereditary coproporphyria, structural effects of mutations, overview
additional information
-
construction of enzyme-deficient DELTA sll1185 mutant, which fails to grow under aerobic conditions, with accumulation of coproporphyrin III. This growth defect is restored by cultivation under micro-oxic conditions
additional information
construction of enzyme-deficient DELTA sll1185 mutant, which fails to grow under aerobic conditions, with accumulation of coproporphyrin III. This growth defect is restored by cultivation under micro-oxic conditions
additional information
seedlings homozygous for a null mutation in the cpx1 gene completely lack chlorophyll and develop necrotic lesions in the light
additional information
seedlings homozygous for a null mutation in the cpx1 gene completely lack chlorophyll and develop necrotic lesions in the light
additional information
-
seedlings homozygous for a null mutation in the cpx1 gene completely lack chlorophyll and develop necrotic lesions in the light
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Sorianello, E.M.; Mazzetti, M.B.
Function and structure of rat hepatic coproporphyrinogen oxidase
Comp. Biochem. Physiol. B
127
155-164
2000
Rattus sp.
brenda
Jones, M.A.; He, J.; Lash, T.D.
Kinetic studies of novel di- and tri-propionate substrates for the chicken red blood cell enzyme coproporphyrinogen oxidase
J. Biochem.
131
201-205
2002
Gallus gallus
brenda
Gross, U.; Puy, H.; Kuhnel, U.; Meissauer, U.; Deybach, J.C.; Jacob, K.; Martasek, P.; Nordmann, Y.; Doss, M.O.
Molecular, immunological, enzymatic and biochemical studies of coproporphyrinogen oxidase deficiency in a family with hereditary coproporphyria
Cell. Mol. Biol.
48
49-55
2002
Homo sapiens
brenda
Mock, H.P; Heller, W.; Molina, A.; Neubohn, B.; Sandermann, H.; Grimm, B.
Expression of uroporphyrinogen decarboxylase or coproporphyrinogen oxidase antisense RNA in tobacco induces pathogen defense responses conferring increased resistance to tobacco mosaic virus
J. Biol. Chem.
274
4231-4238
1999
Nicotiana tabacum
brenda
Narita, S.; Taketani, S.; Inokuchi, H.
Oxidation of protoporphyrinogen IX in Escherichia coli is mediated by the aerobic coproporphyrinogen oxidase
Mol. Gen. Genet.
261
1012-1020
1999
Escherichia coli
brenda
Martasek, P.; Camadro, J.M.; Raman, R.S.; Lecomte, M.C.; Le Caer, J.P.; Demeler, B.; Grandchamp, B.; Labbe, P.
Human coproporphyrinogen oxidase. Biochemical characterization of recombinant normal and R231W mutated enzymes expressed in E. coli as soluble, catalytically active homodimers
Cell. Mol. Biol.
43
47-58
1997
Homo sapiens
brenda
Yoshinaga, T.
Purification and properties of coproporphyrinogen III oxidase from bovine liver
Methods Enzymol.
281
355-367
1997
Bos taurus, Mus musculus
brenda
Jones, M.A.; Hamilton, M.L.; Lash, T.D.
Effect of covalent modification on coproporphyrinogen oxidase from chicken red blood cells
Prep. Biochem. Biotechnol.
27
47-57
1997
Gallus gallus
brenda
Medlock, A.E.; Dailey, H.A.
Human coproporphyrinogen oxidase is not a metalloprotein
J. Biol. Chem.
271
32507-32510
1996
Homo sapiens
brenda
Kohno, H.; Furukawa, T.; Yoshinaga, T.; Tokunaga, R.; Taketani, S.
Coproporhyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation
J. Biol. Chem.
268
21359-21363
1993
Bos taurus, Mus musculus
brenda
Kohno, H.; Furukawa, T.; Tokunaga, R.; Taketani, S.; Yoshinaga, T.
Mouse coprophorphyrinogen oxidase is a copper-containing enzyme: expression in E. coli and site-directed mutagenesis
Biochim. Biophys. Acta
1292
156-162
1996
Mus musculus
brenda
Hill, K.L.; Merchant, S.
Coordinate expression of coproporphyrinogen oxidase and cytochrome c6 in the green alga Chlamydomonas reinhardtii in response to changes in copper availability
EMBO J.
14
857-865
1995
Chlamydomonas reinhardtii
brenda
Troup, B.; Hungerer, C.; Jahn, D.
Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase
J. Bacteriol.
177
3326-3331
1995
Escherichia coli
brenda
Bogard, M.; Camadro, J.M.; Labbe, P.
Purification and properties of mouse liver coproporphyrinogen oxidase
Eur. J. Biochem.
181
417-421
1989
Mus musculus
brenda
Zagorec, M.; Buhler, J.M.; Treich, I.; Keng, T.; Guarente, L.; Labbe-Bois, R.
Isolation, sequence, and regulation by oxygen of the yeast hem13 gene coding for coproporphyrinogen oxidase
J. Biol. Chem.
263
9718-9724
1988
Saccharomyces cerevisiae
brenda
Al-Hazimi, H.M.G.; Jackson, A.H.; Knight, D.W.; Lash, T.D.
Synthetic and biosynthetic studies of porphyrins. Part 7. The Action of coproporphyrinogen oxidase on coproporphyrinogen-IV: Syntheses of protoporphyrin-XII, mesoporphyrin XIII, and related tricarboxylic porphyrins
J. Chem. Soc. Perkin Trans. I
1987
265-276
1987
Gallus gallus
-
brenda
Li, F.; Lim, C.K.; Peters, T.J.
A high-performance-liquid-chromatographic method for the assay of coproporphyrinogen oxidase activity in rat liver
Biochem. J.
239
481-484
1986
Rattus sp.
brenda
Camadro, J.M.; Chambon, H.; Jolles, J.; Labbe, P.
Purification and properties of coproporphyrinogen oxidase from yeast Saccharomyces cerevisiae
Eur. J. Biochem.
156
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1986
Saccharomyces cerevisiae
brenda
Robinson, J.A.; McDonald, E.; Battersby, A.R.
Biosynthesis of porphyrins and related macrocycles. Part 25. Synthesis of analogues of coproporphyrinogen-III and studies of their interaction with coproporphyrinogen-III oxidase from Euglena gracilis
J. Chem. Soc. Perkin Trans. I
1985
1699-1709
1985
Euglena gracilis
-
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Seehra, J.S.; Jordan, P.M.; Akhtar, M.
Anaerobic and aerobic coproporphyrinogen III oxidases of Rhodopseudomonas spheroids. Mechanism and stereochemistry of vinyl group formation
Biochem. J.
209
709-718
1983
Cereibacter sphaeroides
brenda
Keithly, J.H.; Nadler, K.D.
Protoporphyrin formation in Rhizobium japonicum
J. Bacteriol.
154
838-845
1983
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Homo sapiens
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Synechocystis sp. PCC 6803
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Loskove, Y.; Yasuda, M.; Chen, B.; Nazarenko, I.; Cody, N.; Desnick, R.J.
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Homo sapiens (P36551), Homo sapiens
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Homo sapiens
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