Virtual screening for binding of phenylalanine analogues to phenylalanyl-tRNA synthetase

Journal of the American Chemical Society

Volumn 124, Issue 48, 2002, Pages 14442-14449

  Wang, Pin ^a   Vaidehi, Nagarajan ^a,b   Tirrell, David A ^a   Goddard III, William A ^a,b  

^a California Institute of Technology   (United States)

^b CALIFORNIA INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOSYNTHESIS; CRYSTAL STRUCTURE; ESCHERICHIA COLI;

LIGANDS;

AMINO ACIDS;

AMINO ACID DERIVATIVE; PHENYLALANINE DERIVATIVE; PHENYLALANINE TRANSFER RNA LIGASE;

ARTICLE; CALCULATION; CLINICAL PROTOCOL; CRYSTAL STRUCTURE; ENERGY; ENZYME SUBSTRATE; ESCHERICHIA COLI; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; THERMUS THERMOPHILUS;

AMINO ACID SEQUENCE; BINDING SITES; ESCHERICHIA COLI; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; P-FLUOROPHENYLALANINE; PHENYLALANINE; PHENYLALANINE-TRNA LIGASE; PROTEIN CONFORMATION; THERMODYNAMICS; THERMUS THERMOPHILUS;

EID: 0037021485     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0175441     Document Type: Article

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39. m)b. However, the energies obtained from the HierDock method refer only to the binding event and do not take into account changes in the activation energy of the catalytic step. If we apply the Fersht treatment to the data in Table 5, the values of ΔΔG are 1.35 and 2.13 kcal/mol for 3-thienylalanine and p-fluorophenyl-alanine, respectively. The latter value is in excellent agreement with that reported by Gabius et al. (Gabius, H. J.; von der Haar, F.; Cramer, F. Biochemistry 1983, 22, 2331-2339).
40. m)b. However, the energies obtained from the HierDock method refer only to the binding event and do not take into account changes in the activation energy of the catalytic step. If we apply the Fersht treatment to the data in Table 5, the values of ΔΔG are 1.35 and 2.13 kcal/mol for 3-thienylalanine and p-fluorophenyl-alanine, respectively. The latter value is in excellent agreement with that reported by Gabius et al. (Gabius, H. J.; von der Haar, F.; Cramer, F. Biochemistry 1983, 22, 2331-2339).