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1: Appl Environ Microbiol. 1999 Oct;65(10):4399-403.Click here to read Click here to read Links

Purification and characterization of monovalent cation-activated levodione reductase from Corynebacterium aquaticum M-13.

Wada M, Yoshizumi A, Nakamori S, Shimizu S.

Department of Bioscience, Fukui Prefectural University, 4-1-1 Kenjyojima, Fukui 910-1195, Japan. masaru@fpu.ac.jp

(6R)-2,2,6-Trimethyl-1,4-cyclohexanedione (levodione) reductase was isolated from a cell extract of the soil isolate Corynebacterium aquaticum M-13. This enzyme catalyzed regio- and stereoselective reduction of levodione to (4R,6R)-4-hydroxy-2,2, 6-trimethylcyclohexanone (actinol). The relative molecular mass of the enzyme was estimated to be 142,000 Da by high-performance gel permeation chromatography and 36,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme required NAD(+) or NADH as a cofactor, and it catalyzed reversible oxidoreduction between actinol and levodione. The enzyme was highly activated by monovalent cations, such as K(+), Na(+), and NH(4)(+). The NH(2)-terminal and partial amino acid sequences of the enzyme showed that it belongs to the short-chain alcohol dehydrogenase/reductase family. This is the first report of levodione reductase.

PMID: 10508066 [PubMed - indexed for MEDLINE]

PMCID: PMC91584

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