Occurrence of 5'-deoxyadenosylcobalamin and its physiological function as the coenzyme of methylmalonyl-CoA mutase in a marine eukaryotic microorganism, Schizochytrium limacinum SR21

J Nutr Sci Vitaminol (Tokyo). 2007 Dec;53(6):471-5. doi: 10.3177/jnsv.53.471.

Abstract

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.

MeSH terms

  • Animals
  • Cobamides / chemistry
  • Cobamides / isolation & purification
  • Cobamides / metabolism*
  • Coenzymes / chemistry
  • Coenzymes / isolation & purification
  • Coenzymes / metabolism*
  • Enzyme Activation
  • Eukaryota / enzymology*
  • Fatty Acids / metabolism
  • Methylmalonyl-CoA Mutase / chemistry
  • Methylmalonyl-CoA Mutase / isolation & purification
  • Methylmalonyl-CoA Mutase / metabolism*
  • Molecular Weight
  • Temperature

Substances

  • Cobamides
  • Coenzymes
  • Fatty Acids
  • Methylmalonyl-CoA Mutase
  • cobamamide