The crystal structure of human Δ4-3-ketosteroid 5β-reductase defines the functional role of the residues of the catalytic tetrad in the steroid double bond reduction mechanism

Biochemistry

Volumn 47, Issue 32, 2008, Pages 8261-8270

  Faucher, Frédérick ^a,b   Cantin, Line ^a   Luu The, Van ^a   Labrie, Fernand ^a   Breton, Rock ^a  

^a LAVAL UNIVERSITY   (Canada)

^b UNIVERSITY OF VERMONT COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; ENZYME ACTIVITY; HORMONES;

ACTIVE SITES; BILE ACIDS; DOUBLE BONDS; REDUCTION MECHANISMS; SEQUENCE ALIGNMENTS; STEREOSPECIFIC MANNER; STEROID HORMONES;

CRYSTAL STRUCTURE;

3ALPHA HYDROXYSTEROID DEHYDROGENASE; 7ALPHA HYDROXYCHOLESTEROL; BILE ACID; DRUG RESIDUE; GLUTAMIC ACID; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXOSTEROID; PROGESTERONE DERIVATIVE; STEROID 5BETA REDUCTASE; TYROSINE;

ARTICLE; CATALYSIS; CHEMICAL BOND; DRUG BINDING; ENZYME STRUCTURE; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; REDUCTION;

BINDING SITES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; KETOSTEROIDS; OXIDATION-REDUCTION; OXIDOREDUCTASES; TESTOSTERONE 5-ALPHA-REDUCTASE;

EID: 49449111950     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800572s     Document Type: Article

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