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Titolo:
NAD-DEPENDENT D-2-HYDROXYISOCAPROATE DEHYDROGENASE OF LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS - GENE CLONING AND ENZYME CHARACTERIZATION()
Autore:
BERNARD N; JOHNSEN K; FERAIN T; GARMYN D; HOLS P; HOLBROOK JJ; DELCOUR J;
Indirizzi:
UNIV CATHOLIQUE LOUVAIN,DEPT BIOL,UNITE GENET,BATIMENT CLAUDE BERNARD,PL CROIX SUD,5 BTE 6 B-1348 LOUVAIN BELGIUM UNIV CATHOLIQUE LOUVAIN,DEPT BIOL,UNITE GENET B-1348 LOUVAIN BELGIUM UNIV BRISTOL,CTR MOLEC RECOGNIT BRISTOL ENGLAND UNIV BRISTOL,DEPT BIOCHEM BRISTOL ENGLAND
Titolo Testata:
European journal of biochemistry
fascicolo: 2, volume: 224, anno: 1994,
pagine: 439 - 446
SICI:
0014-2956(1994)224:2<439:NDDOL>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-LACTATE DEHYDROGENASE; LIGAND-BINDING SITES; ESCHERICHIA-COLI; STEREOSPECIFIC REDUCTION; 2-KETOCARBOXYLIC ACIDS; VANCOMYCIN RESISTANCE; EXPRESSION; FRAMEWORK; PROTEINS; CASEI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
N. Bernard et al., "NAD-DEPENDENT D-2-HYDROXYISOCAPROATE DEHYDROGENASE OF LACTOBACILLUS-DELBRUECKII SUBSP BULGARICUS - GENE CLONING AND ENZYME CHARACTERIZATION()", European journal of biochemistry, 224(2), 1994, pp. 439-446

Abstract

A genomic library from Lactobacillus delbrueckii subsp. bulgaricus was used to complement an Escherichia coli mutant strain deficient for both lactate dehydrogenase and pyruvate formate lyase, and thus unable to grow anaerobically. One recombinant clone was found to display a broad specificity NAD(+)-dependent D-2-hydroxyacid dehydrogenase activity. The corresponding gene (named hdhD) was subcloned and sequenced. The deduced amino acid sequence of the encoded enzyme indicates a 333-residue protein closely related to D-2-hydroxyisocaproate (i.e. 2-hydroxy-4-methyl-pentanoate) dehydrogenase (D-HO-HxoDH) of Lactobacillus casei and other NAD(+)-dependent D-lactate dehydrogenases (D-LDH) from several other bacterial species. The hdhD gene was overexpressed under the control of the lambda phage P-L promoter and the enzyme was purified with a two-step method. The L. delbrueckii subsp. bulgaricus enzyme,like that of L. casei, was shown to be active on a wide variety of 2-oxoacid substrates except those having a branched beta-carbon.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 00:13:02