Thermostabilization of Pichia stipitis xylitol dehydrogenase by mutation of structural zinc-binding loop

Journal of Biotechnology

Volumn 129, Issue 4, 2007, Pages 717-722

  Annaluru, Narayana ^a   Watanabe, Seiya ^a   Pack, Seung Pil ^a   Saleh, Ahmed Abu ^a   Kodaki, Tsutomu ^a   Makino, Keisuke ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Site directed mutagenesis; Structural zinc; Thermostability; Xylitol dehydrogenase

Indexed keywords

DEHYDROGENASE; DENATURATION TEMPERATURE; MUTANTS; PICHIA STIPITIS;

DENATURATION; ENZYME KINETICS; MUTAGENESIS; THERMODYNAMIC STABILITY; ZINC;

YEAST;

ALCOHOL; IDITOL DEHYDROGENASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG; XYLITOL DEHYDROGENASE; XYLOSE; ZINC;

ARTICLE; COMPARATIVE STUDY; ENZYME DENATURATION; ENZYME STRUCTURE; FERMENTATION; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PICHIA STIPITIS; PRIORITY JOURNAL; PROTEIN FAMILY; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; WILD TYPE;

AMINO ACID SEQUENCE; BINDING SITES; D-XYLULOSE REDUCTASE; ENZYME STABILITY; FUNGAL PROTEINS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PICHIA; PROTEIN CONFORMATION; THERMODYNAMICS; ZINC;

PICHIA STIPITIS;

EID: 34247173915     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.02.006     Document Type: Article

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