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

EC Number:

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

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the opposite direction.

In Pathways: adenosylcobalamin biosynthesis II (late cobalt incorporation) , 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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