Participation of Histidine-51 in Catalysis by Horse Liver Alcohol Dehydrogenase

Biochemistry

Volumn 43, Issue 11, 2004, Pages 3014-3026

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

^a UNIVERSITY OF IOWA   (United States)

^b F HOFFMANN LA ROCHE LTD   (Switzerland)

^c Mogam Biotechnology Research Institute   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; ALDEHYDES; CATALYSIS; CHARGE TRANSFER; COMPLEXATION; CONFORMATIONS; HYDROGEN BONDS; ISOMERIZATION; OXIDATION; PH EFFECTS; RATE CONSTANTS; REDUCTION;

DEPROTONATION; HYDRIDE TRANSFER;

ENZYMES;

2,3 DIFLUOROBENZYL ALCOHOL; 2,4 DIFLUOROBENZYL ALCOHOL; ACETALDEHYDE; ADENOSINE PHOSPHATE; ALCOHOL; ALCOHOL DEHYDROGENASE; BENZYL ALCOHOL DERIVATIVE; DEUTERIUM; GLUTAMINE; HISTIDINE; HYDROXYL GROUP; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG; WATER; ZINC;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; ENZYME KINETICS; HORSE; HYDROGEN BOND; ISOMERIZATION; MOLECULAR INTERACTION; OXIDATION; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTON TRANSPORT; REDUCTION; STEADY STATE; X RAY CRYSTALLOGRAPHY;

ALCOHOL DEHYDROGENASE; AMINO ACID SUBSTITUTION; ANIMALS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DEUTERIUM EXCHANGE MEASUREMENT; GLUTAMINE; HISTIDINE; HORSES; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; LIVER; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NAD;

EQUUS CABALLUS;

EID: 1542743968     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi036103m     Document Type: Article

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