Substrate selectivity and biochemical properties o...[Appl Environ Microbiol. 1998]

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1: Appl Environ Microbiol. 1998 Oct;64(10):4093-4. Links

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

Pollard JR, Rialland D, Bugg TD.

Department of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, United Kingdom.

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.

PMID: 9758851 [PubMed - indexed for MEDLINE]

PMCID: PMC106610

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Biochemistry. 1981 Apr 28; 20(9):2497-502.

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Enzyme stereoselectivity: the reversible reaction catalyzed by 2-keto-4-hydroxyglutarate aldolase of Escherichia coli.
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Cited by 2 PubMed Central articles

Identification of a hydratase and a class II aldolase involved in biodegradation of the organic solvent tetralin.
Hernáez MJ, Floriano B, Ríos JJ, Santero E. Appl Environ Microbiol. 2002 Oct; 68(10):4841-6.

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ReviewBiodegradation of aromatic compounds by Escherichia coli.
Díaz E, Ferrández A, Prieto MA, García JL. Microbiol Mol Biol Rev. 2001 Dec; 65(4):523-69, table of contents.

[Microbiol Mol Biol Rev. 2001]

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