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Titolo:
CLONING AND EXPRESSION OF THE GENE FOR HYDROXYPYRUVATE REDUCTASE (D-GLYCERATE DEHYDROGENASE FROM AN OBLIGATE METHYLOTROPH HYPHOMICROBIUM-METHYLOVORUM-GM2
Autore:
YOSHIDA T; YAMAGUCHI K; HAGISHITA T; MITSUNAGA T; MIYATA A; TANABE T; TOH H; OHSHIRO T; SHIMAO M; IZUMI Y;
Indirizzi:
KINKI UNIV,FAC AGR,DEPT FOOD & NUTR,NAKA MACHI NARA 631 JAPAN NATL CARDIOVASC CTR,RES INST,DEPT PHARMACOL OSAKA JAPAN KYUSHU INST TECHNOL,DEPT BIOCHEM ENGN KITAKYUSHU FUKUOKA JAPAN TOTTORI UNIV,FAC ENGN,DEPT BIOTECHNOL TOTTORI 680 JAPAN
Titolo Testata:
European journal of biochemistry
fascicolo: 3, volume: 223, anno: 1994,
pagine: 727 - 732
SICI:
0014-2956(1994)223:3<727:CAEOTG>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-LACTATE DEHYDROGENASE; ACID DEHYDROGENASES; FORMATE DEHYDROGENASE; ESCHERICHIA-COLI; ACTIVE-SITE; SEQUENCE; ALIGNMENT; REGIONS; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
T. Yoshida et al., "CLONING AND EXPRESSION OF THE GENE FOR HYDROXYPYRUVATE REDUCTASE (D-GLYCERATE DEHYDROGENASE FROM AN OBLIGATE METHYLOTROPH HYPHOMICROBIUM-METHYLOVORUM-GM2", European journal of biochemistry, 223(3), 1994, pp. 727-732

Abstract

The gene encoding hydroxppyruvate reductase, catalyzing the asymmetric reduction of hydroxypyruvate to D-glycerate, and its flanking regions were isolated from a methylotrophic bacterium, Hyphomicrobium merthylovorum GM2. Nucleotide sequencing of the recombinant plasmids revealed that the hydroxypyruvate-reductase gene codes for the 322-amino-acidprotein with calculated molecular mass 35726 Da. The sequence was confirmed by sequencing the intact enzyme and peptides obtained by digestion of the enzyme with Achromobacter proteinase I, The amino acid sequence of the enzyme showed similarity to members of the D-isomer-specific 2-hydroxyacid dehydrogenase family. The recombinant plasmid, which was constructed by ligation of the cloned gene and an expression vector pKK223-3, was introduced into Escherichia coli HB101. The recombinant enzyme purified from the transformed E. coli cells was indistinguishable from the enzyme isolated from H. methylovorum GM2 by immunological and enzymological analyses.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 15:52:52