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. 1974 Jun;118(3):890–897. doi: 10.1128/jb.118.3.890-897.1974

Specificity and Induction of Undecyl Acetate Esterase from Pseudomonas cepacia Grown on 2-Tridecanone

A C Shum 1, A J Markovetz 1
PMCID: PMC246836  PMID: 4208413

Abstract

Undecyl acetate esterase from Pseudomonas cepacia grown on 2-tridecanone was strongly inhibited by organophosphates and other esterase inhibitors. Also, p-chloromercuribenzoate at 1 × 10−4 M showed a 70% inhibition of esterase activity. The enzyme hydrolyzed both aliphatic and aromatic acetate esters at substrate concentrations of 0.25 M. Under these conditions the highest reaction rate was toward undecyl acetate. No lipase or proteolytic activity was demonstrated. Undecyl acetate esterase was classified as a carboxylesterase (B-esterase). Cell-free activity studies on the production of undecyl acetate esterase grown on different carbon sources plus zymogram studies demonstrated that the enzyme was inducible when 2-tridecanone, 2-tridecanol, undecyl acetate and, to a lesser extent, 1-undecanol were growth substrates. Induction of undecyl acetate esterase during oxidation of 2-tridecanone supports the view that undecyl acetate is an intermediate in the degradation of the methyl ketone.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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