The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits

Biochemistry

Volumn 38, Issue 42, 1999, Pages 13829-13836

  Anderson, Amy C ^a   O'Neil, Robert H ^a   DeLano, Warren L ^a,b   Stroud, Robert M ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Sunesis Pharmaceuticals Inc   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CATALYSIS; CHEMICAL BONDS; CLONING; CONFORMATIONS; CRYSTALLIZATION; DNA; MOLECULAR STRUCTURE; MONOMERS; ORGANIC COMPOUNDS; PROTEINS; PURIFICATION;

DEOXYTHYMIDINE MONOPHOSPHATE; DNA REPLICATION; PATHOGEN; PNEUMOCYSTIS CARINII; THYMIDYLATE SYNTHASE;

ENZYME KINETICS;

BACTERIAL ENZYME; DEOXYURIDINE PHOSPHATE; THYMIDYLATE SYNTHASE;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; PNEUMOCYSTIS CARINII; PRIORITY JOURNAL;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DEOXYURACIL NUCLEOTIDES; DIMERIZATION; ENZYME ACTIVATION; ENZYME INHIBITORS; FOLIC ACID; LIGANDS; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PNEUMOCYSTIS; PROTEIN CONFORMATION; QUINAZOLINES; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; THYMIDYLATE SYNTHASE;

EID: 0345426287     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi991610i     Document Type: Article

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