Crystal structure of a thermophilic alcohol dehydrogenase substrate complex suggests determinants of substrate specificity and thermostability

Proteins: Structure, Function and Genetics

Volumn 37, Issue 4, 1999, Pages 619-627

  Li, Chunmin ^a,b   Heatwole, Joel ^a   Soelaiman, Sandriyana ^a   Shoham, Menachem ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

Crystallography; Enzyme; Extremophile; Heat stable; Substrate binding

Indexed keywords

ALCOHOL DEHYDROGENASE; HYDROGEN; ZINC ION;

ARTICLE; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME BINDING; ENZYME SPECIFICITY; HIGH TEMPERATURE; HYDROGEN BOND; MELTING POINT; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

BACTERIA (MICROORGANISMS); CLOSTRIDIUM BEIJERINCKII; THERMOANAEROBACTER BROCKII;

EID: 0032703356     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<619::AID-PROT12>3.0.CO;2-H     Document Type: Article

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