PMID:9758851

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Citation

Pollard, JR, Rialland, D and Bugg, TD (1998) Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli. Appl. Environ. Microbiol. 64:4093-4

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.

Links

PubMed PMC106610

Keywords

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

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