Uptake and physiological function of vitamin B12 in a photosynthetic unicellular coccolithophorid alga, Pleurochrysis carterae

Biosci Biotechnol Biochem. 2002 Jan;66(1):195-8. doi: 10.1271/bbb.66.195.

Abstract

The photosynthetic coccolithophoid alga, Pleurochrysis (Hymenomonas) carterae, could take up and accumulate exogenous vitamin B12, most of which was converted into the coenzyme forms of vitamin B12. Two vitamin B12-dependent enzyme activities (methylmalonyl-CoA mutase, 2.6+/-0.4 nmol/min/mg protein and methionine synthase, 85.1+/-38.9 pmol/min/mg protein) could be found in a cell homogenate of the vitamin B12-supplemented alga. Most of the methylmalonyl-CoA mutase activity and 19.2% of the vitamin B12 accumulated by the algal cells were recovered in the macromolecular fractions with Mr of 150 kDa, although the remaining vitamin B12 was found only in free vitamin B12 fractions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / metabolism
  • Cobamides / metabolism
  • Eukaryota / metabolism*
  • Methylmalonyl-CoA Mutase / metabolism
  • Photosynthesis
  • Vitamin B 12 / isolation & purification
  • Vitamin B 12 / metabolism
  • Vitamin B 12 / physiology*

Substances

  • Cobamides
  • 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
  • Methylmalonyl-CoA Mutase
  • cobamamide
  • Vitamin B 12