Cloning and over-expression in Escherichia coli of the gene encoding NADPH group III alcohol dehydrogenase from Thermococcus hydrothermalis. Characterization and comparison of the native and the recombinant enzymes

European Journal of Biochemistry

Volumn 264, Issue 3, 1999, Pages 880-889

  Antoine, Elisabeth ^a   Rolland, Jean Luc ^b   Raffin, Jean Paul ^b   Dietrich, Jacques ^b  

^a IFREMER   (France)

^b NONE

Author keywords

Alcohol dehydrogenase; NADP dependent; Over expression; pH dependent structure; Thermophilic

Indexed keywords

ALCOHOL DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE OVEREXPRESSION; MOLECULAR CLONING; PRIORITY JOURNAL; STRUCTURE ANALYSIS; THERMOCOCCUS; THERMOCOCCUS HYDROTHERMALIS;

ALCOHOL DEHYDROGENASE; AMINO ACID SEQUENCE; BASE SEQUENCE; CLONING, MOLECULAR; DIMERIZATION; DNA, ARCHAEAL; ENZYME STABILITY; ESCHERICHIA COLI; GENE EXPRESSION; GENES, ARCHAEAL; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; NADP; OLIGONUCLEOTIDE PROBES; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; THERMOCOCCUS;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; PROKARYOTA; THERMOCOCCUS HYDROTHERMALIS;

EID: 0033568692     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00685.x     Document Type: Article

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