A catalytic consensus motif for D-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens

Biochemical Journal

Volumn 367, Issue 1, 2002, Pages 13-18

  Klimacek, Mario ^a   Nidetzky, Bernd ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

Author keywords

Alcohol dehydrogenase; Chemical mechanism; Polyol specific long chain dehydrogenase

Indexed keywords

AMINO ACIDS; CATALYSIS; FRUCTOSE; OXIDATION; SOLVENTS;

KINETIC PARAMETERS;

ENZYMES;

ALCOHOL DEHYDROGENASE; ASPARAGINE; HISTIDINE; LYSINE; MANNITOL DEHYDROGENASE; POLYOL; ISOTOPE; MANNITOL; MANNITOL 2 DEHYDROGENASE (NADP); MANNITOL 2-DEHYDROGENASE (NADP); RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; ENZYME ANALYSIS; ENZYME SPECIFICITY; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN PURIFICATION; PSEUDOMONAS FLUORESCENS; SITE DIRECTED MUTAGENESIS; STEREOCHEMISTRY; CHEMISTRY; ENZYME ACTIVE SITE; ENZYMOLOGY; KINETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PH; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION;

PSEUDOMONAS; PSEUDOMONAS FLUORESCENS;

ALCOHOL DEHYDROGENASE; ALCOHOL OXIDOREDUCTASES; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ASPARAGINE; CATALYTIC DOMAIN; CONSERVED SEQUENCE; HYDROGEN-ION CONCENTRATION; ISOTOPES; KINETICS; LYSINE; MANNITOL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN STRUCTURE, TERTIARY; PSEUDOMONAS FLUORESCENS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0036797834     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020932     Document Type: Article

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