Occurrence of 5'-deoxyadenosylcobalamin and its physiological function as the coenzyme of methylmalonyl-CoA mutase in a marine eukaryotic microorganism, Schizochytrium limacinum SR21.
A marine eukaryotic microorganism, Schizochytrium limacinum SR21, had the ability to absorb and accumulate exogenous cobalamin, which was converted to the cobalamin coenzymes 5'-deoxyadenosylcobalamin (20.1%) and methylcobalamin (29.6%). A considerably high activity (about 38 mU/mg protein) of 5'-deoxyadenosylcobalamin-dependent methylmalonyl-CoA mutase (EC 5.4.99.2) involved in amino acid and odd-chain fatty acid metabolism was found in the cell homogenate of S. limacinum SR21. The enzyme was purified to homogeneity and characterized.
Miyamoto
Emi
E
Department of Health and Nutrition, Nagasaki International University, Sasebo, Japan. miyamo@niu.ac.jp
Tanioka
Yuri
Y
Yukino
Tsugiyo
T
Hayashi
Masahiro
M
Watanabe
Fumio
F
Nakano
Yoshihisa
Y
D000818:Animals; D003038:Cobamides / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D003067:Coenzymes / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004789:Enzyme Activation; D056890:Eukaryota / Q000201:enzymology*; D005227:Fatty Acids / Q000378:metabolism; D008765:Methylmalonyl-CoA Mutase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D013696:Temperature
D003038:Cobamides; D003067:Coenzymes; D005227:Fatty Acids; D008765:Methylmalonyl-CoA Mutase; C000913:cobamamide