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Titolo:
NAD(+)-dependent (S)-specific secondary alcohol dehydrogenase involved in stereoinversion of 3-pentyn-2-ol catalyzed by Norcardia fusca AKU 2123
Autore:
Xie, SX; Ogawa, J; Shimizu, S;
Indirizzi:
Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 Life Sci, Sakyo Ku, Kyoto 6068502, Japan
Titolo Testata:
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
fascicolo: 10, volume: 63, anno: 1999,
pagine: 1721 - 1729
SICI:
0916-8451(199910)63:10<1721:N(SADI>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
CARBONYL REDUCTASE; RHODOCOCCUS-ERYTHROPOLIS; ETHYL 4-CHLORO-3-OXOBUTANOATE; CANDIDA-PARAPSILOSIS; ALDEHYDE REDUCTASE; PURIFICATION; HYDROLYSIS; ESTERS; YEAST;
Keywords:
secondary alcohol dehydrogenase; stereoinversion; Nocardia fusca; acetylenic alcohol; stereospecific reduction;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
24
Recensione:
Indirizzi per estratti:
Indirizzo: Shimizu, S Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 Sakyo Ku, Kyoto 6068502, Japan
Citazione:
S.X. Xie et al., "NAD(+)-dependent (S)-specific secondary alcohol dehydrogenase involved in stereoinversion of 3-pentyn-2-ol catalyzed by Norcardia fusca AKU 2123", BIOS BIOT B, 63(10), 1999, pp. 1721-1729

Abstract

An NAD(+)-dependent alcohol dehydrogenase was purified to homogeneity fromNocardia fusca AKU 2123. The enzyme catalyzed (S)-specific oxidation of 3-pentyn-2-ol(PYOH), i.e., part of the stereoinversion reaction for the production of (R)-PYOH, which is a valuable chiral building block for pharmaceuticals, from the racemate. The enzyme used a broad variety of secondary alcohols including alkyl alcohols, alkenyl alcohols, acetylenic alcohols, and aromatic alcohols as substrates. The oxidation was (S)isomer specific in every case. The K-m and V-max for (S)-PYOH and (S)-2-hexanol oxidation were 1.6 mM and 53 mu mol/min/mg, and 0.33 mM and 130 mu mol/min/mg, respectively. The enzyme also catalyzed stereoselective reduction of carbonyl compounds. (S)-2-Hexanol and ethyl (R)-4-chloro-3-hydroxybutanoate in high optical purity were produced from 2-hexanone and ethyl 4-chloro-3-oxobutanoate by thepurified enzyme, respectively. The K-m and V-max for 2-hexanone reduction were 2.5 mM and 260 mu mol/min/mg. The enzyme has a relative molecular massof 150,000 and consists of four identical subunits. The NH2-terminal aminoacid sequence of the enzyme shows similarity:with those of the carbonyl reductase from Rhodococcus erythropolis and phenylacetaldehyde reductase fromCorynebacterium sp.

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Documento generato il 21/09/20 alle ore 06:12:14