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. 1988 Apr 15;251(2):461–466. doi: 10.1042/bj2510461

Purification and characterization of diacetyl-reducing enzymes from Staphylococcus aureus.

I Vidal 1, J González 1, A Bernardo 1, R Martín 1
PMCID: PMC1149025  PMID: 3041963

Abstract

A method was developed to purify diacetyl-reducing enzymes from Staphylococcus aureus. Two enzymes capable of catalysing diacetyl reduction were isolated, neither of which turned out to be a specific diacetyl reductase. One of them is a lactate dehydrogenase similar to the one from Staphylococcus epidermidis, which accepts diacetyl, although poorly. The other one uses as coenzyme beta-NAD and reduces uncharged alpha-dicarbonyls with more than three carbon atoms (especially the alpha-diketones diacetyl and pentane-2,3-dione), producing the L(+) form of the corresponding alpha-hydroxycarbonyls. This enzyme has an Mr of 68,000 and is, most probably, a monomer. Its optimum pH is 6.0. Its shows a high affinity for NADH and a rather low one for diacetyl, which, at least in vitro, does not seem to be as good a substrate as pentane-2,3-dione. We propose for it the systematic name L-alpha-hydroxyketone:NAD+ oxidoreductase and the recommended name of alpha-diketone reductase (NAD). We also suggest that the diacetyl reductase entry in the I.U.B. classification be suppressed.

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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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