Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli.
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.
Department of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, United Kingdom.
J R
JR
Pollard
D
D
Rialland
T D
TD
Bugg
D000079:Acetaldehyde / Q000378:metabolism; D000446:Aldehyde-Lyases / Q000378:metabolism*; D002087:Butyrates / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D010667:Phenylpyruvic Acids / Q000378:metabolism; D013379:Substrate Specificity
D002087:Butyrates; D010667:Phenylpyruvic Acids; C005087:alpha-ketobutyric acid; C115453:4-hydroxy-2-ketopentanoic acid aldolase; D000446:Aldehyde-Lyases; D000079:Acetaldehyde; C031606:phenylpyruvic acid