Study of the mechanism of action of adenosylcobalamindependent glycerol dehydratase from Aerobacter aerogenes. II. The inactivation kinetics of glycerol dehydratase complexes with adenosylobalamin and its analogs

Biochim Biophys Acta. 1977 Sep 15;484(1):236-43. doi: 10.1016/0005-2744(77)90128-0.

Abstract

The inactivation kinetics of vacterial glycerol dehydratase (EC 4.2.1.30) in the course of its reaction with adenosylcobalamin (AdoCbl) and its analogs were investigated. It was shown that the inactivation rate of apoenzyme complexes with AdoCbl analogs is determined by the nature of the analogs employed and probably by the rate of their conversion into hydroxycobalamins. A possible inactivation mechanism of glycerol dehydratase is discussed.

MeSH terms

  • Apoenzymes / metabolism
  • Chemical Phenomena
  • Chemistry
  • Cobamides / metabolism
  • Cobamides / pharmacology*
  • Enterobacter / enzymology*
  • Enterobacteriaceae / enzymology*
  • Glycerol
  • Hydro-Lyases / antagonists & inhibitors*
  • Hydro-Lyases / metabolism
  • Kinetics
  • Mathematics
  • Structure-Activity Relationship

Substances

  • Apoenzymes
  • Cobamides
  • Hydro-Lyases
  • Glycerol