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.
Debussche
L
L
Département Analyse, Centre de Recherche de Vitry-Alfortville, Vitry-sur-Seine, France.
Couder
M
M
Thibaut
D
D
Cameron
B
B
Crouzet
J
J
Blanche
F
F
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