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Titolo:
2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family
Autore:
Bonete, MJ; Ferrer, J; Pire, C; Penades, M; Ruiz, JL;
Indirizzi:
Univ Alicante, Fac Ciencias, Dept Bioquim, E-03080 Alicante, Spain Univ Alicante Alicante Spain E-03080 pt Bioquim, E-03080 Alicante, Spain
Titolo Testata:
BIOCHIMIE
fascicolo: 12, volume: 82, anno: 2000,
pagine: 1143 - 1150
SICI:
0300-9084(200012)82:12<1143:2DFHMA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-LACTATE DEHYDROGENASE; N-TERMINAL SEQUENCE; GLUTAMATE-DEHYDROGENASE; ENZYME-PURIFICATION; D-2-HYDROXYISOCAPROATE DEHYDROGENASE; L-2-HYDROXYISOCAPROATE DEHYDROGENASE; STEREOSPECIFIC REDUCTION; HALOBACTERIUM-HALOBIUM; 2-KETOCARBOXYLIC ACIDS; LACTOBACILLUS-CONFUSUS;
Keywords:
Archaea; Haloferax mediterranei; D-hydroxyacid dehydrogenase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Bonete, MJ Univ Alicante, Fac Ciencias, Dept Bioquim, Ap 99, E-03080 Alicante, Spain Univ Alicante Ap 99 Alicante Spain E-03080 080 Alicante, Spain
Citazione:
M.J. Bonete et al., "2-Hydroxyacid dehydrogenase from Haloferax mediterranei, a D-isomer-specific member of the 2-hydroxyacid dehydrogenase family", BIOCHIMIE, 82(12), 2000, pp. 1143-1150

Abstract

An NAD-dependent D-2-hydroxyacid dehydrogenase (EC 1.1.1.) was isolated and characterized from the halophilic Archaeon Haloferax mediterranei. The enzyme is a dimer with a molecular mass of 101.4 +/- 3.3 kDa. It is strictly NAD-dependent and exhibits its highest activity in 4 M NaCl. The enzyme is characterized by a broad substrate specificity 2-ketoisocaproate and 2-ketobutyrate being the substrates with the higher V-max/K-m. When pyruvate and 2-ketobutyrate were the substrates the optimal pH was acidic (pH 5) meanwhile for 2-ketoisocaproate maximum activity was achieved at basic pH between 7.5 and 8.5. The optimum temperature was 52 degreesC and at 65 degreesC there was a pronounced activity decrease. This new enzyme can be used for the production of D-2-hydroxycarboxylic acid. (C) 2000 Societe francaise de biochimie et biologie moleculaire / Editions scientifiques et medicales Elsevier SAS.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 00:07:28