Purification and partial characterization of Cob(I)alamin adenosyltransferase from Pseudomonas denitrificans.
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.
Département Analyse, Centre de Recherche de Vitry-Alfortville, Vitry-sur-Seine, France.
L
L
Debussche
M
M
Couder
D
D
Thibaut
B
B
Cameron
J
J
Crouzet
F
F
Blanche
D019883:Alkyl and Aryl Transferases; D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity; D014166:Transferases / Q000737:chemistry / Q000302:isolation & purification*
D014166:Transferases; D019883:Alkyl and Aryl Transferases; C019920:cob(I)alamin adenosyltransferase