Purification and characterization of Cob(II)yrinic acid a,c-diamide reductase from Pseudomonas denitrificans.
An NADH-dependent flavoenzyme exhibiting cob(II)yrinic acid a,c-diamide reductase activity was purified 6,300-fold to homogeneity from Pseudomonas denitrificans and sequenced at its N terminus. This enzyme of the cobalamin biosynthetic pathway reduced to the Co(I) state all of the Co(II)-corrinoids isolated from this microorganism.
Blanche
F
F
Département Analyse, Rhône-Poulenc Rorer S.A., Vitry-sur-Seine, France.
Maton
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L
Debussche
L
L
Thibaut
D
D
D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008970:Molecular Weight; D009247:NADH, NADPH Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity
D009247:NADH, NADPH Oxidoreductases; C078110:cob(II)yrinic acid a,c-diamide reductase