Affiliation:
1. Département Analyse, Centre de Recherche de Vitry-Alfortville, Vitry-sur-Seine, France.
Abstract
Cob(I)alamin adenosyltransferase (EC 2.5.1.17) was purified to homogeneity from extracts of a Pseudomonas denitrificans recombinant strain and sequenced at its N terminus. It is a homodimer (each unit with an Mr of 28,000) encoded by cobO. The enzyme adenosylated all of the corrinoids isolated from this microorganism but did not adenosylate cobyrinic acid.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Reference16 articles.
1. Zur chemie und biochemie der corrinoide. XXIX. Biogenesewege von der cobyrinsaure und zum cobinamid bei Propionibacterium shermanii;Bernhauer K.;Hoppe-Seyler's Z. Physiol. Chem.,1968
2. Biosynthesis of vitamin B12: stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c-diamide is catalyzed by one enzyme in Pseudomonas denitrificans;Blanche F.;J. Bacteriol.,1991
3. Purification and characterization of S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase from Pseudomonas denitrificans;Blanche F.;J. Bacteriol.,1989
4. Identification and quantitation of corrinoid precursors of cobalamin from Pseudomonas denitrificans by high-performance liquid chromatography;Blanche F.;Anal. Biochem.,1990
5. Hydrogenobyrinic acid: isolation, biosynthesis and function;Blanche F.;Angew. Chem. Int. Ed. Engl.,1990
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