Recent advances in elucidation of biological corrinoid functions

FEMS Microbiol Rev. 1993 Nov;12(4):349-65. doi: 10.1111/j.1574-6976.1993.tb00027.x.

Abstract

Eleven adenosylcorrinoid-dependent rearrangements and elimination reactions have been described during the last four decades of vitamin B12 research. In contrast, only the cobamide-dependent methionine synthase was well established as a corrinoid-dependent methyl transfer reaction. yet, investigations during the last few years revealed nine additional corrinoid-dependent methyltransferases. Many of these reactions are catalyzed by bacteria which possess a distinct C1 metabolism. Notably acetogenic and methanogenic bacteria carry out such methyl transfers in their anabolism and catabolism. Tetrahydrofolate or a similar pterine derivative is a key intermediate in these reactions. It functions as methyl acceptor and the methylated tetrahydrofolate serves as a methyl donor.

Publication types

  • Review

MeSH terms

  • 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase / metabolism
  • Acetates / metabolism
  • Bacteria / metabolism
  • Corrinoids
  • Euryarchaeota / metabolism
  • Humans
  • Methane / metabolism
  • Methyltransferases / metabolism*
  • Porphyrins / chemistry
  • Porphyrins / metabolism*
  • Tetrahydrofolates / metabolism*

Substances

  • Acetates
  • Corrinoids
  • Porphyrins
  • Tetrahydrofolates
  • Methyltransferases
  • 5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase
  • Methane
  • 5-methyltetrahydrofolate