The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer

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Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling. © 2010 The Royal Society of Chemistry.

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Detalles Bibliográficos
Autor principal: Stojkovic, V.
Otros Autores: Perissinotti, L.L, Lee, J., Benkovic, S.J, Kohen, A.
Formato: Capítulo de libro
Lenguaje:Inglés
Publicado: 2010
Acceso en línea:Registro en Scopus
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Registro en la Biblioteca Digital
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Biblioteca Central Dr. Luis F. Leloir (FCEN) de Universidad de Buenos Aires
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024 7 |2 cas  |a alanine, 56-41-7, 6898-94-8; dihydrofolate reductase, 9002-03-3; hydrogen, 12385-13-6, 1333-74-0; isoleucine, 7004-09-3, 73-32-5; Alanine, 56-41-7; Isoleucine, 73-32-5; NADP, 53-59-8; Tetrahydrofolate Dehydrogenase, 1.5.1.3 
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100 1 |a Stojkovic, V. 
245 1 4 |a The effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer 
260 |c 2010 
270 1 0 |m Kohen, A.; Department of Chemistry, University of Iowa, Iowa City, IA, United States; email: amnon-kohen@uiowa.edu 
504 |a Basran, J., Masgrau, L., Sutcliffe, M.J., Scrutton In, N.S., (2006) Isotope Effects in Chemistry and Biology, pp. 671-689. , A. Kohen and H. H. Limbach, ed., Taylor & Francis, CRC Press, Boca Raton, FL 
504 |a Kohen In, A., (2006) Isotope Effects in Chemistry and Biology, pp. 743-764. , A. Kohen and H. H. Limbach, ed., Taylor & Francis, CRC Press, Boca Raton, FL 
504 |a Nagel, Z.D., Klinman, J.P., (2006) Chem. Rev., 106, pp. 3095-3118 
504 |a Wang, L., Goodey, N.M., Benkovic, S.J., Kohen, A., (2006) Proc. Natl. Acad. Sci. U. S. A., 103, pp. 15753-15758 
504 |a Truhlar In, D.G., (2006) Isotope Effects in Chemistry and Biology, pp. 579-620. , A. Kohen and H. H. Limbach, ed., Taylor & Francis, CRC Press, Boca Raton, FL 
504 |a Hammes-Schiffer, S., (2006) Acc. Chem. Res., 39, pp. 93-100 
504 |a Warshel, A., Olsson, M.H.M., Villá-Freixa, J., (2006) Isotope Effects in Chemistry and Biology, pp. 621-644. , A. Kohen and H. H. Limbach, ed., Taylor & Francis, CRC Press, Boca Raton, FL 
504 |a Wang, L., Tharp, S., Selzer, T., Benkovic, S.J., Kohen, A., (2006) Biochemistry, 45, pp. 1383-1392 
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504 |a Garcia-Viloca, M., Truhlar, D.G., Gao, J., (2003) Biochemistry, 42, pp. 13558-13575 
504 |a Schwartz In, S.D., (2006) Isotope Effects in Chemistry and Biology, pp. 475-498. , A. Kohen and H. H. Limbach, ed., Taylor & Francis, CRC Press, Boca Raton, FL 
504 |a Kuznetsov, A., Ulstrup, J., (1999) Can. J. Chem., 77, pp. 1085-1096 
504 |a Kiefer, P.M., Hynes In, J.T., (2006) Isotope Effects in Chemistry and Biology, pp. 549-578. , A. Kohen and H. H. Limbach, ed., Taylor & Francis, CRC Press, Boca Raton, FL 
504 |a Sawaya, M.R., Kraut, J., (1997) Biochemistry, 36, pp. 586-603 
504 |a Boehr, D.D., McElheny, D., Dyson, H.J., Wright, P.E., (2006) Science, 313, pp. 1638-1642 
504 |a Case, D.A., Darden, T.A., Cheatham, T.E., Simmerling, C.L., Wang, J., Duke, R.E., Luo, R., Kollman, P.A., (2006), University of California, San Francisco; Fierke, C.A., Johnson, K.A., Benkovic, S.J., (1987) Biochemistry, 26, pp. 4085-4092 
504 |a Adams, J.A., Fierke, C.A., Benkovic, S.J., (1991) Biochemistry, 30, pp. 11046-11054 
506 |2 openaire 
520 3 |a Comparison of the nature of hydride transfer in wild-type and active site mutant (I14A) of dihydrofolate reductase suggests that the size of this side chain at position 14 modulates H-tunneling. © 2010 The Royal Society of Chemistry.  |l eng 
593 |a Department of Chemistry, University of Iowa, Iowa City, IA, United States 
593 |a Departamento de Química Inorgánica, Analítica y Química Física, INQUIMAE, Ciudad Universitaria, Pabellón II piso 3, C1428EHA Buenos Aires, Argentina 
593 |a Department of Chemistry, Pennsylvania State University, University Park, PA, United States 
690 1 0 |a ALANINE 
690 1 0 |a DIHYDROFOLATE REDUCTASE 
690 1 0 |a HYDROGEN 
690 1 0 |a ISOLEUCINE 
690 1 0 |a ARTICLE 
690 1 0 |a BIOTRANSFORMATION 
690 1 0 |a CATALYSIS 
690 1 0 |a CHEMICAL REACTION 
690 1 0 |a CRYSTAL STRUCTURE 
690 1 0 |a MOLECULAR DYNAMICS 
690 1 0 |a QUANTUM MECHANICS 
690 1 0 |a SITE DIRECTED MUTAGENESIS 
690 1 0 |a SYNTHESIS 
690 1 0 |a ALANINE 
690 1 0 |a AMINO ACID SUBSTITUTION 
690 1 0 |a CATALYSIS 
690 1 0 |a CATALYTIC DOMAIN 
690 1 0 |a ESCHERICHIA COLI 
690 1 0 |a ISOLEUCINE 
690 1 0 |a KINETICS 
690 1 0 |a MOLECULAR DYNAMICS SIMULATION 
690 1 0 |a MUTATION 
690 1 0 |a NADP 
690 1 0 |a TETRAHYDROFOLATE DEHYDROGENASE 
700 1 |a Perissinotti, L.L. 
700 1 |a Lee, J. 
700 1 |a Benkovic, S.J. 
700 1 |a Kohen, A. 
773 0 |d 2010  |g v. 46  |h pp. 8974-8976  |k n. 47  |p Chem. Commun.  |x 13597345  |w (AR-BaUEN)CENRE-1038  |t Chemical Communications 
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856 4 0 |u https://doi.org/10.1039/c0cc02988b  |y DOI 
856 4 0 |u https://hdl.handle.net/20.500.12110/paper_13597345_v46_n47_p8974_Stojkovic  |y Handle 
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