Explaining an unusually fast parasitic enzyme: Folate tail-binding residues dictate substrate positioning and catalysis in Cryptosporidium hominis thymidylate synthase

Biochemistry

Volumn 47, Issue 34, 2008, Pages 8902-8911

  Martucci, W Edward ^a   Vargo, Melissa A ^a   Anderson, Karen S ^a  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; CATALYSIS; CHEMOTHERAPY; CHLORINE COMPOUNDS; DRUG DELIVERY; DRUG DOSAGE; DRUG INTERACTIONS; ENZYMES; FOOD ADDITIVES;

ACTIVE SITES; BINDING RESIDUES; CATALYTIC CYCLING; CATALYTIC STATE; CONFORMATIONAL CHANGES; CRYPTOSPORIDIUM HOMINIS; DRUG DESIGNS; INCREASED FLEXIBILITY; LONG-RANGE INTERACTIONS; RAPID RATE; STRUCTURAL DATA; THYMIDYLATE SYNTHASE; WATER NETWORKS;

LIGANDS;

FOLIC ACID; THYMIDYLATE SYNTHASE;

A287F GENE; A287F/S290G GENE; ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYPTOSPORIDIUM HOMINIS; CRYSTAL STRUCTURE; ENZYME ACTIVITY; GENE MUTATION; GENE STRUCTURE; MUTANT; NONHUMAN; PRIORITY JOURNAL; S290G GENE; STRUCTURE ANALYSIS;

ANIMALS; BINDING SITES; CATALYSIS; CRYPTOSPORIDIUM; CRYSTALLOGRAPHY, X-RAY; MULTIENZYME COMPLEXES; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTOZOAN PROTEINS; TETRAHYDROFOLATE DEHYDROGENASE; THYMIDYLATE SYNTHASE;

CRYPTOSPORIDIUM HOMINIS;

EID: 50149113480     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800466z     Document Type: Article

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