The only active mutant of thymidylate synthase D169, a residue far from the site of methyl transfer, demonstrates the exquisite nature of enzyme specificity

Protein Engineering

Volumn 16, Issue 3, 2003, Pages 229-240

  Birdsall, David L ^a   Finer Moore, Janet ^a   Stroud, Robert M ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

5,10 methylenetetrahydrofolate; Bi substrate reactions; dUMP; Hydrogen bond; Negative cooperativity

Indexed keywords

10 PROPARGYL 5,8 DIDEAZAFOLIC ACID; ASPARTIC ACID; CARBOXYL GROUP; CYSTEINE; DEOXYURIDINE PHOSPHATE; FOLIC ACID ANTAGONIST; METHYLENETETRAHYDROFOLIC ACID; MUTANT PROTEIN; THYMIDYLATE SYNTHASE; THYMIDYLATE SYNTHASE D169; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; COMPLEX FORMATION; COVALENT BOND; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STABILITY; ESCHERICHIA COLI; HYDROGEN BOND; PRIORITY JOURNAL; X RAY ANALYSIS;

DEOXYURACIL NUCLEOTIDES; DIMERIZATION; ENZYME STABILITY; MUTATION; PROTEIN CONFORMATION; THYMIDYLATE SYNTHASE;

ESCHERICHIA COLI;

EID: 0037880473     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

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