Role of an invariant lysine residue in folate binding on Escherichia coli thymidylate synthase: Calorimetric and crystallographic analysis of the K48Q mutant

International Journal of Biochemistry and Cell Biology

Volumn 40, Issue 10, 2008, Pages 2206-2217

  Arvizu Flores, Aldo A ^a   Sugich Miranda, Rocio ^b   Arreola, Rodrigo ^c   Garcia Orozco, Karina D ^a   Velazquez Contreras, Enrique F ^b   Montfort, William R ^d   Maley, Frank ^e   Sotelo Mundo, Rogerio R ^a  

^a CENTRO DE INVESTIGACIÓN EN ALIMENTACIÓN Y DESARROLLO   (Mexico)

^b UNIVERSIDAD DE SONORA   (Mexico)

^c INSTITUTO DE FISIOLOGÍA CELULAR   (Mexico)

^d UNIVERSITY OF ARIZONA   (United States)

^e WADSWORTH CENTER   (United States)

Author keywords

Isothermal titration calorimetry; Mutant K48Q; Protein crystallography; Thymidylate synthase; Tryptophan fluorescence

Indexed keywords

10 PROPARGYL 5,8 DIDEAZAFOLIC ACID; 2 [5 [[(1,2 DIHYDRO 3 METHYL 1 OXOBENZO[F]QUINAZOLIN 9 YL)METHYL]AMINO] 1 OXO 2 ISOINDOLINYL]GLUTARIC ACID; DEOXYURIDINE PHOSPHATE; ENZYME INHIBITOR; FOLIC ACID; K48 PROTEIN; LYSINE; METHYLENETETRAHYDROFOLIC ACID; MUTANT PROTEIN; NUCLEOTIDE; PROPARGYLDIDEAZAFOLATE; THYMIDYLATE SYNTHASE;

ARTICLE; BINDING AFFINITY; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENTHALPY; ENTROPY; ENZYME ACTIVITY; ENZYME INHIBITION; ESCHERICHIA COLI; ISOTHERMAL TITRATION CALORIMETRY; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; STEREOISOMERISM; STRUCTURE ANALYSIS; WILD TYPE;

AMINO ACID SUBSTITUTION; BINDING SITES; CALORIMETRY; CATALYSIS; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; FOLIC ACID; FOLIC ACID ANTAGONISTS; LIGANDS; LYSINE; MUTANT PROTEINS; MUTATION; NUCLEOTIDES; PROTEIN STRUCTURE, SECONDARY; STRUCTURE-ACTIVITY RELATIONSHIP; TETRAHYDROFOLATES; THERMODYNAMICS; THYMIDYLATE SYNTHASE; TRYPTOPHAN;

ESCHERICHIA COLI;

EID: 48949116938     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2008.02.025     Document Type: Article

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