Identification of aspartic acid-203 in human thymidine phosphorylase as an important residue for both catalysis and non-competitive inhibition by the small molecule "crystallization chaperone" 5′-O-tritylinosine (KIN59)

Biochemical Pharmacology

Volumn 78, Issue 3, 2009, Pages 231-240

  Bronckaers, A ^a   Aguado, L ^b   Negri, A ^c   Camarasa, M J ^b   Balzarini, J ^a   Perez Perez M J ^b   Gago, F ^c   Liekens, S ^a  

^a REGA INSTITUTE FOR MEDICAL RESEARCH   (Belgium)

^b INSTITUTO DE QUÍMICA MÉDICA   (Spain)

^c UNIVERSITY OF ALCALÁ   (Spain)

Author keywords

5 O Tritylinosine (KIN59); Allosteric inhibitor; Modeling; Mutagenesis; Thymidine phosphorylase

Indexed keywords

5' O TRITYLINOSINE; 6 AMINO 5 BROMOURACIL; 6 AMINOTHYMINE; AMINO ACID; ASPARTIC ACID; BLOCKING AGENT; INOSINE DERIVATIVE; KIN 59; THYMIDINE PHOSPHORYLASE; UNCLASSIFIED DRUG;

ARTICLE; CANCER THERAPY; CATALYSIS; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; CRYSTALLIZATION; DRUG BINDING SITE; DRUG POTENTIATION; DRUG STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE; HUMAN; HYDROGEN BOND; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN ANALYSIS; SIMULATION; SITE DIRECTED MUTAGENESIS; WILD TYPE; X RAY;

AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ACID; CATALYTIC DOMAIN; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; HUMANS; HYDROGEN BONDING; INOSINE; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; SEQUENCE HOMOLOGY, AMINO ACID; THYMIDINE PHOSPHORYLASE; TRITYL COMPOUNDS;

EID: 65749085724     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bcp.2009.04.011     Document Type: Article

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