The putative coenzyme B12-dependent methylmalonyl-CoA mutase from potatoes is a phosphatase.
The reported presence of a coenzyme B12-dependent methylmalonyl-CoA mutase in potatoes has been reexamined. The enzyme converting methylmalonyl-CoA was purified to electrophoretic homogeneity. Examination of the reaction product by 1H, 31P NMR and mass spectrometry revealed that it was methylmalonyl-3'-dephospho-CoA. The phosphatase enzyme needs neither coenzyme B12 nor S-adenosylmethionine as a cofactor.
Paizs
Csaba
C
Department of Biochemistry and Biochemical Engineering, Babeş-Bolyai University, 400028-Arany János 11, Cluj-Napoca (Kolozsvár), Romania.
Diemer
Tanja
T
Rétey
János
J
D003038:Cobamides / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry / Q000379:methods; D008765:Methylmalonyl-CoA Mutase / Q000737:chemistry* / Q000302:isolation & purification*; D008956:Models, Chemical; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry*; D011198:Solanum tuberosum / Q000201:enzymology*; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D013696:Temperature
D003038:Cobamides; D010744:Phosphoric Monoester Hydrolases; D008765:Methylmalonyl-CoA Mutase; C000913:cobamamide