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Biochemistry

Volumn 39, Issue 42, 2000, Pages 12885-12897

Structural basis for substrate specificity differences of horse liver alcohol dehydrogenase isozymes

(7) Adolph, H W a Zwart, P b Meijers, R b Hubatsch, I a,d Kiefer, M a Lamzin, V b Cedergren Zeppezauer, E c

a SAARLAND UNIVERSITY (Germany)

b EUROPEAN MOLECULAR BIOLOGY LABORATORY (Germany)

c LUND UNIVERSITY (Sweden)

d UPPSALA UNIVERSITY (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

5BETA ANDROSTANOLONE; ALCOHOL; ALCOHOL DEHYDROGENASE; ANDROSTANEDIOL; ISOENZYME; KETONE; LIVER ENZYME; NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID SUBSTITUTION; ARTICLE; CRYSTAL STRUCTURE; ENZYME CONFORMATION; ENZYME POLYMORPHISM; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HORSE; NONHUMAN; PRIORITY JOURNAL; STEREOCHEMISTRY;

ALCOHOL DEHYDROGENASE; AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CHOLIC ACID; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ELECTRONS; HORSES; ISOENZYMES; KINETICS; LIVER; MICROSPECTROPHOTOMETRY; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NAD; STEREOISOMERISM; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EQUUS CABALLUS;

EID: 0034711039 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi001376s Document Type: Article

Times cited : (34)

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