Enzyme

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     6. Ligases
        6.6 Forming nitrogen-D-metal bonds
            6.6.1 Forming coordination complexes
ID:6.6.1.2
Description:Cobaltochelatase.
Alternative Name: Hydrogenobyrinic acid a,c-diamide cobaltochelatase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 6.6.1.2
BRENDA Enzyme Link: BRENDA 6.6.1.2
KEGG Enzyme Link: KEGG6.6.1.2
BioCyc Enzyme Link: BioCyc 6.6.1.2
ExPASy Enzyme Link: ExPASy6.6.1.2
EC2PDB Enzyme Link: EC2PDB 6.6.1.2
ExplorEnz Enzyme Link: ExplorEnz 6.6.1.2
PRIAM enzyme-specific profiles Link: PRIAM 6.6.1.2
IntEnz Enzyme Link: IntEnz 6.6.1.2
MEDLINE Enzyme Link: MEDLINE 6.6.1.2
MSA:

6.6.1.2;

Phylogenetic Tree:

6.6.1.2;

Uniprot:
M-CSA:
RHEA:15341 ATP + Co(2+) + H2O + hydrogenobyrinate a,c-diamide = ADP + cob(II)yrinate a,c diamide + 5 H(+) + phosphate
RULE(radius=1) [*:1]-[C;H0;+0:2]1=[C;H0;+0:3]2-[*:4]-[*:5]-[C;H0;+0:6](=[N;H0;+0:7]-2)-[CH;+0:8]=[C;H0;+0:9]2-[*:10]-[*:11]-[C;H0;+0:12](=[N;H0;+0:13]-2)-[C;H0;+0:14](-[*:15])=[C;H0;+0:16](-[*:17])-[NH;+0:18]-[*:19]-[*:20]-[N;H0;+0:21]=[C;H0;+0:22]-1-[*:23].[*:24]=[P;H0;+0:25](-[*:26])(-[*:27])-[O;H0;+0:28]-[*:29].[Co+2;H0:30].[OH2;+0:31]>>[*:1]-[C;H0;+0:2]1=[C;H0;+0:22](-[*:23])-[N;H0;+0:21]2-[*:20]-[*:19]-[N+;H0:18]3=[C;H0;+0:16](-[*:17])-[C;H0;+0:14](-[*:15])=[C;H0;+0:12]4-[*:11]-[*:10]-[C;H0;+0:9]5=[N+;H0:13]-4-[Co-2;H0:30]-3-2-[N+;H0:7]2=[C;H0;+0:3]-1-[*:4]-[*:5]-[C;H0;+0:6]-2=[CH;+0:8]-5.[*:29]-[OH;+0:28].[*:24]=[P;H0;+0:25](-[*:26])(-[*:27])-[OH;+0:31]
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References

TitleAuthorsDatePubMed ID
Assay, purification, and characterization of cobaltochelatase, a unique complex enzyme catalyzing cobalt insertion in hydrogenobyrinic acid a,c-diamide during coenzyme B12 biosynthesis in Pseudomonas denitrificans.Debussche L, Couder M, Thibaut D, Cameron B, Crouzet J, Blanche F1992 Nov1429466
The biosynthesis of adenosylcobalamin (vitamin B12).Warren MJ, Raux E, Schubert HL, Escalante-Semerena JC2002 Aug12195810