Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli

Appl Environ Microbiol. 1998 Oct;64(10):4093-4. doi: 10.1128/AEM.64.10.4093-4094.1998.

Abstract

4-Hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli was identified as a class I aldolase. The enzyme was found to be highly selective for the acetaldehyde acceptor but would accept alpha-ketobutyric acid or phenylpyruvic acid in place of the pyruvic acid carbonyl donor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetaldehyde / metabolism
  • Aldehyde-Lyases / metabolism*
  • Butyrates / metabolism
  • Escherichia coli / enzymology*
  • Kinetics
  • Phenylpyruvic Acids / metabolism
  • Substrate Specificity

Substances

  • Butyrates
  • Phenylpyruvic Acids
  • alpha-ketobutyric acid
  • 4-hydroxy-2-ketopentanoic acid aldolase
  • Aldehyde-Lyases
  • Acetaldehyde
  • phenylpyruvic acid