Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer

Biochemistry

Volumn 38, Issue 42, 1999, Pages 13951-13959

  Ramaswamy, S ^a   Park, Doo Hong ^b,c   Plapp, Bryce V ^b  

^a SWEDISH UNIVERSITY OF AGRICULTURAL SCIENCES   (Sweden)

^b UNIVERSITY OF IOWA   (United States)

^c Mogam Biotechnology Research Institute   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; AMINO ACIDS; CATALYSIS; CHEMICAL BONDS; CONFORMATIONS; DISSOCIATION; HYDROGEN; MUTAGENESIS; OXIDATION; STRUCTURE (COMPOSITION); SUBSTITUTION REACTIONS; X RAY CRYSTALLOGRAPHY;

ACETALDEHYDE; FLEXIBLE LOOP; HORSE LIVER ALCOHOL DEHYDROGENASE; NICOTINAMIDE RIBOSE MOIETY; TRIFLUOROETHANOL;

ENZYMES;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME KINETICS; ENZYME MODIFICATION; MOLECULAR MODEL; PRIORITY JOURNAL; PROTON TRANSPORT; SITE DIRECTED MUTAGENESIS; X RAY CRYSTALLOGRAPHY;

ALANINE; ALCOHOL DEHYDROGENASE; AMINO ACID SUBSTITUTION; ANIMALS; CRYSTALLOGRAPHY, X-RAY; ELECTRON TRANSPORT; ENZYME ACTIVATION; GLYCINE; HORSES; HYDROGEN; KINETICS; LIVER; MUTAGENESIS, SITE-DIRECTED; PROLINE; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY; THREONINE;

EID: 0344631780     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991731i     Document Type: Article

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