Asp-99 donates a hydrogen bond not to Tyr-14 but to the steroid directly in the catalytic mechanism of Δ5-3-ketosteroid isomerase from Pseudomonas putida biotype B

Biochemistry

Volumn 39, Issue 5, 2000, Pages 903-909

  Choi, Gildon ^a   Ha, Nam Chul ^a   Kim, Suhng Wook ^a,b   Kim, Do Hyung ^a   Park, Songhee ^a   Oh, Byung Ha ^a   Choi, Kwan Yong ^a  

^a Pohang University of Science and Technology (POSTECH)   (South Korea)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; OXOSTEROID; STEROID; STEROID DELTA ISOMERASE; TYROSINE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIFFUSION; HYDROGEN BOND; ISOMERISM; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; PSEUDOMONAS PUTIDA; SITE DIRECTED MUTAGENESIS;

ASPARAGINE; ASPARTIC ACID; BINDING SITES; CATALYSIS; EQUILENIN; GLUTAMIC ACID; HYDROGEN BONDING; KINETICS; MACROMOLECULAR SUBSTANCES; MUTAGENESIS, SITE-DIRECTED; NANDROLONE; PSEUDOMONAS PUTIDA; STEROID ISOMERASES; TYROSINE;

BACTERIA (MICROORGANISMS); FELIS CATUS; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0034620560     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991579k     Document Type: Article

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