Kinetic investigations with inhibitors that mimic the posthomolysis intermediate in the reactions of coenzyme-B12-dependent glycerol dehydratase and diol dehydratase

László Poppe, János Rétey

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Kinetic investigations were performed on the coenzyme-B12-dependent glycerol dehydratase and diol dehydratase reactions using 1,2-propanediol as substrate and [ω(adenosin-5'-O-yl)alkyl]cobalamins as mimics of the posthomolysis intermediate slate of the coenzyme. All the coenzyme-B12 analogues with oligomethylene chains (C3-C7) inserted between the central Co atom and the 5' O of the adenosine moiety were competitive inhibitors with respect to coenzyme B12. The apparent inhibition constants (K(i)) of the shorter-chain inhibitors, especially the C5 inhibitor, were smaller for both enzymes than those of the longer-chain (C6, C7) compounds. These results are in agreement with the expected (0.6-0.9 nm) distance between the Co and 5'-methylene paramagnetic centers in the posthomolysis intermediate state of coenzyme B12 in these reactions.

Original languageEnglish
Pages (from-to)398-401
Number of pages4
JournalEuropean Journal of Biochemistry
Volume245
Issue number2
DOIs
Publication statusPublished - Jan 1 1997

    Fingerprint

Keywords

  • Analogues of coenzyme B
  • Glycerol dehydratase
  • Kinetic investigation
  • Propanediol dehydratase
  • [ω(adenosine-5'-O-yl)alkyl]cobalamin

ASJC Scopus subject areas

  • Biochemistry

Cite this