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Titolo:
CLONING, SEQUENCING, AND EXPRESSION IN ESCHERICHIA-COLI OF THE GENE CODING FOR PHOSPHOFRUCTOKINASE IN LACTOBACILLUS-BULGARICUS
Autore:
BRANNY P; DELATORRE F; GAREL JR;
Indirizzi:
CNRS,ENZYMOL LAB F-91198 GIF SUR YVETTE FRANCE CNRS,ENZYMOL LAB F-91198 GIF SUR YVETTE FRANCE
Titolo Testata:
Journal of bacteriology
fascicolo: 17, volume: 175, anno: 1993,
pagine: 5344 - 5349
SICI:
0021-9193(1993)175:17<5344:CSAEIE>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-LACTATE DEHYDROGENASE; SITE-DIRECTED MUTAGENESIS; NUCLEOTIDE-SEQUENCE; BACILLUS-STEAROTHERMOPHILUS; THERMUS-THERMOPHILUS; MOLECULAR-CLONING; PYRUVATE-KINASE; HIGH-LEVEL; ENZYME; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
P. Branny et al., "CLONING, SEQUENCING, AND EXPRESSION IN ESCHERICHIA-COLI OF THE GENE CODING FOR PHOSPHOFRUCTOKINASE IN LACTOBACILLUS-BULGARICUS", Journal of bacteriology, 175(17), 1993, pp. 5344-5349

Abstract

A fragment of 1,185 bp containing the gene coding for phosphofructokinase (ATP:D-fructose-6-phosphate-1-phosphotransferase; EC 2.7.1.11) inLactobacillus bulgaricus has been cloned, sequenced, and expressed inEscherichia coli. The amino acid sequence of this enzyme was homologous to those of the ATP-dependent phosphofructokinases from E. coli, Thermus thermophilus, Spiroplasma citri, and Bacillus stearothermophilus, suggesting that these enzymes have closely related structures despite their different regulatory properties. The recombinant protein had the same structural and functional properties as did the original enzyme. The 3' end of the 1,185-bp fragment showed the presence of an open reading frame corresponding to the N-terminal amino acid sequence of the pyruvate kinase from L. bulgaricus. This gene organization, the same as that in S. citri (C. Chevalier, C. Saillard, and J. M. Bove, J. Bacteriol. 172:2693-2703, 1990) and B. stearothermophilus (D. Walker, W. N. Chia, and H. Muirhead, J. Mol. Biol. 228:265-276, 1992; H. Sakai and T. Ohta, Eur. J. Biochem. 311:851-859, 1993) but different from that in E. coli (H. W. Hellinga and P. R. Evans, Eur. J. Biochem. 149:363-373, 1985), indicated that the same transcription unit apparently contained the genes for phosphofructokinase and pyruvate kinase, the twokey enzymes of glycolysis. The possibility that these genes could be transcribed at the same time suggested that in L. bulgaricus, the coordinated regulation of phosphofructokinase and pyruvate kinase occurs at the levels of both biosynthesis and enzymatic activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:44:24