MetaCyc Enzyme: cob(II)yrinate a,c-diamide reductase

Species: Pseudomonas denitrificans

Subunit composition of cob(II)yrinate a,c-diamide reductase = [cob(II)yrinate a,c-diamide reductase subunit]2

An NADH-dependent flavoenzyme exhibiting cob(II)yrinate a,c-diamide reductase activity was purified 6,300-fold to homogeneity from Pseudomonas denitrificans [Blanche92]. The enzyme reduces the bound Co2+ ion to Co1+. Even though the first 6 amino acids have been determined (MEKTRL), the gene encoding this enzyme has not been identified, and the enzyme has not been characterized any further.

A gene that matches this sequence was later discovered in Brucella melitensis, and the enzyme it encodes has been characterized (see cob(II)yrinate a,c-diamide reductase).

Molecular Weight of Polypeptide: 16.0 kD (experimental) [Blanche92]

Molecular Weight of Multimer: 30 kD (experimental) [Blanche92]

Gene-Reaction Schematic

Gene-Reaction Schematic

Created 22-Jan-2001 by Pellegrini-Toole A, Marine Biological Laboratory
Revised 28-Jun-2007 by Caspi R, SRI International

Enzymatic reaction of: cob(II)yrinate a,c-diamide reductase

Inferred from experiment

EC Number:

2 cob(I)yrinate a,c-diamide + FMN + 3 H+ ← 2 cob(II)yrinate a,c-diamide + FMNH2

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

The reaction is favored in the opposite direction.

In Pathways: adenosylcobalamin biosynthesis II (aerobic), adenosylcobalamin biosynthesis from cobyrinate a,c-diamide II, adenosylcobalamin biosynthesis from cobyrinate a,c-diamide I

Cofactors or Prosthetic Groups: FAD [Blanche92]


Blanche92: Blanche F, Maton L, Debussche L, Thibaut D (1992). "Purification and characterization of Cob(II)yrinic acid a,c-diamide reductase from Pseudomonas denitrificans." J Bacteriol 1992;174(22);7452-4. PMID: 1429467

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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