Use of anion-aromatic interactions to position the general base in the ketosteroid isomerase active site

Proceedings of the National Academy of Sciences of the United States of America

Volumn 110, Issue 28, 2013, Pages 11308-11313

  Schwans, Jason P ^a   Sunden, Fanny ^a   Lassila, Jonathan K ^a   Gonzalez, Ana ^b   Tsai, Yingssu ^a,b   Herschlag, Daniel ^a  

^a STANFORD UNIVERSITY   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

Author keywords

Enzyme catalysis; General base catalysis; Noncovalent interactions

Indexed keywords

ANION; AROMATIC COMPOUND; ASPARTIC ACID; PHENYLALANINE; STEROID DELTA ISOMERASE;

ARTICLE; CATALYSIS; CHEMICAL INTERACTION; COMAMONAS TESTOSTERONI; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STATIC ELECTRICITY; X RAY CRYSTALLOGRAPHY;

ENZYME CATALYSIS; GENERAL-BASE CATALYSIS; NONCOVALENT INTERACTIONS;

ANIONS; CATALYTIC DOMAIN; KETOSTEROIDS; MUTATION; STEROID ISOMERASES; X-RAY DIFFRACTION;

COMAMONAS TESTOSTERONI;

EID: 84879969716     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1206710110     Document Type: Article

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