Enzyme

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     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.98 With other, known, physiological acceptors
ID:1.3.98.3
Description:Coproporphyrinogen dehydrogenase.
Alternative Name: Oxygen-independent coproporphyrinogen-III oxidase.
Coproporphyrinogen III oxidase.
Cath: 1.10.10.920; 3.80.30.20;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.98.3
BRENDA Enzyme Link: BRENDA 1.3.98.3
KEGG Enzyme Link: KEGG1.3.98.3
BioCyc Enzyme Link: BioCyc 1.3.98.3
ExPASy Enzyme Link: ExPASy1.3.98.3
EC2PDB Enzyme Link: EC2PDB 1.3.98.3
ExplorEnz Enzyme Link: ExplorEnz 1.3.98.3
PRIAM enzyme-specific profiles Link: PRIAM 1.3.98.3
IntEnz Enzyme Link: IntEnz 1.3.98.3
MEDLINE Enzyme Link: MEDLINE 1.3.98.3
MSA:

1.3.98.3;

Phylogenetic Tree:

1.3.98.3;

Uniprot:
M-CSA:
RHEA:15425 coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX
RULE(radius=1) ([*:1]-[CH2;+0:2]-[CH2;+0:3]-[C;H0;+0:4](=[*:5])-[OH;+0:6].[*:7]=[C;H0;+0:8](-[OH;+0:9])-[CH2;+0:10]-[CH2;+0:11]-[*:12]).[*:13]-[S+;H0:14](-[*:15])-[CH2;+0:16]-[*:17]>>[*:17]-[CH3;+0:16].([*:1]-[CH;+0:2]=[CH2;+0:3].[*:12]-[CH;+0:11]=[CH2;+0:10]).[*:13]-[S;H0;+0:14]-[*:15].[*:7]=[C;H0;+0:8]=[O;H0;+0:9].[*:5]=[C;H0;+0:4]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Functional differentiation of two analogous coproporphyrinogen III oxidases for heme and chlorophyll biosynthesis pathways in the cyanobacterium Synechocystis sp. PCC 6803.Goto T, Aoki R, Minamizaki K, Fujita Y2010 Apr20194361
Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes.Layer G, Moser J, Heinz DW, Jahn D, Schubert WD2003 Dec 114633981
Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli.Layer G, Verfürth K, Mahlitz E, Jahn D2002 Sep 1312114526