Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	4 proteins
Enzyme class ^help_outline	EC 6.6.1.2 cobaltochelatase
GO Molecular Function ^help_outline	GO:0051116 cobaltochelatase activity

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Name ^help_outline hydrogenobyrinate a,c-diamide Identifier CHEBI:77874 Charge -2 Formula C45H60N6O12 InChIKey^help_outline JJMDOVLPFPOLFZ-IPUCCYEASA-L SMILES^help_outline C\C1=C2\N[C@@](C)([C@@H]3[NH+]=C(\C(C)=C4/[NH+]=C(/C=C5\[NH+]=C1[C@@](C)(CC(N)=O)[C@@H]5CCC([O-])=O)C(C)(C)[C@@H]4CCC([O-])=O)[C@](C)(CCC([O-])=O)[C@H]3CC([O-])=O)[C@@](C)(CC(N)=O)[C@@H]2CCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline Co²⁺ Identifier CHEBI:48828 (CAS: 22541-53-3) ^help_outline Charge 2 Formula Co InChIKey^help_outline XLJKHNWPARRRJB-UHFFFAOYSA-N SMILES^help_outline [Co++] 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) ^help_outline Charge -4 Formula C10H12N5O13P3 InChIKey^help_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILES^help_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,284 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H₂O Identifier CHEBI:15377 (CAS: 7732-18-5) ^help_outline Charge 0 Formula H2O InChIKey^help_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILES^help_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline cob(II)yrinate a,c diamide Identifier CHEBI:58537 Charge -4 Formula C45H56CoN6O12 InChIKey^help_outline IADMSJRJSGLGJI-OKJGWHJPSA-H SMILES^help_outline CC1=C2N3[C@H]([C@H](CC([O-])=O)[C@@]2(C)CCC([O-])=O)[C@]2(C)[N+]4=C([C@@H](CCC([O-])=O)[C@]2(C)CC(N)=O)C(C)=C2[N+]5=C(C=C6[N+](=C1[C@@H](CCC([O-])=O)C6(C)C)[Co--]345)[C@@H](CCC([O-])=O)[C@]2(C)CC(N)=O 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) ^help_outline Charge -3 Formula C10H12N5O10P2 InChIKey^help_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILES^help_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 841 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKey^help_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILES^help_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,002 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:15341	RHEA:15342	RHEA:15343	RHEA:15344
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	4 proteins
EC numbers ^help_outline	6.6.1.2
Gene Ontology ^help_outline	GO:0051116
KEGG ^help_outline				R05227
MetaCyc ^help_outline		R342-RXN

Publications

The biosynthesis of adenosylcobalamin (vitamin B12).

Warren M.J., Raux E., Schubert H.L., Escalante-Semerena J.C.

Vitamin B12, or cobalamin, is one of the most structurally complex small molecules made in Nature. Major progress has been made over the past decade in understanding how this synthesis is accomplished. This review covers some of the most important findings that have been made and provides the read ... >> More

Vitamin B12, or cobalamin, is one of the most structurally complex small molecules made in Nature. Major progress has been made over the past decade in understanding how this synthesis is accomplished. This review covers some of the most important findings that have been made and provides the reader with a complete description of the transformation of uroporphyrinogen III into adenosylcobalamin (AdoCbl). 183 references are cited. << Less

Nat Prod Rep 19:390-412(2002) [PubMed] [EuropePMC]

This publication is cited by 16 other entries.
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 F.

Hydrogenobyrinic acid a,c-diamide was shown to be the substrate of cobaltochelatase, an enzyme that catalyzes cobalt insertion in the corrin ring during the biosynthesis of coenzyme B12 in Pseudomonas denitrificans. Cobaltochelatase was demonstrated to be a complex enzyme composed of two different ... >> More

Hydrogenobyrinic acid a,c-diamide was shown to be the substrate of cobaltochelatase, an enzyme that catalyzes cobalt insertion in the corrin ring during the biosynthesis of coenzyme B12 in Pseudomonas denitrificans. Cobaltochelatase was demonstrated to be a complex enzyme composed of two different components of M(r) 140,000 and 450,000, which were purified to homogeneity. The 140,000-M(r) component was shown to be coded by cobN, whereas the 450,000-M(r) component was composed of two polypeptides specified by cobS and cobT. Each component was inactive by itself, but cobaltochelatase activity was reconstituted upon mixing CobN and CobST. The reaction was ATP dependent, and the Km values for hydrogenobyrinic acid a,c-diamide, Co2+, and ATP were 0.085 +/- 0.015, 4.2 +/- 0.2, and 220 +/-36 microM, respectively. Spectroscopic data revealed that the reaction product was cob(II)yrinic acid a,c-diamide, and experiments with a coupled-enzyme incubation system containing both cobaltochelatase and cob(II)yrinic acid a,c-diamide reductase (F. Blanche, L. Maton, L. Debussche, and D. Thibaut, J. Bacteriol. 174:7452-7454, 1992) confirmed this result. This report not only provides the first evidence that hydrogenobyrinic acid and its a,c-diamide derivative are indeed precursors of adenosylcobalamin but also demonstrates that precorrin-6x, precorrin-6y, and precorrin-8x, three established precursors of hydrogenobyrinic acid (D. Thibaut, M. Couder, A. Famechon, L. Debussche, B. Cameron, J. Crouzet, and F. Blanche, J. Bacteriol. 174:1043-1049, 1992), are also on the pathway to cobalamin. << Less

J. Bacteriol. 174:7445-7451(1992) [PubMed] [EuropePMC]

RHEA:15341 hydrogenobyrinate a,c-diamide + Co(2+) + ATP + H2O = cob(II)yrinate a,c diamide + ADP + phosphate + 5 H(+)

Enzymes

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Cross-references

Publications

The biosynthesis of adenosylcobalamin (vitamin B12).

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.