TY - JOUR
T1 - The structural enzymology of proton-transfer reactions
AU - Petsko, Gregory
AU - Ringe, Dagmar
AU - Allen, Karen
AU - Lavie, Arnon
AU - Gerhart-Mueller, Eva
AU - Clifton, James
AU - Hasson, Miriam
AU - Fujita, Shigeo
AU - Sugio, Shigetoshi
AU - Xhang, Xidhong
AU - Davenport, Robert
AU - Lolis, Elias
AU - Neidhart, David
AU - Kenyon, George
AU - Gerlt, John
AU - Bash, Paul
AU - Knowles, Jeremy
AU - Karplus, Martin
N1 - Funding Information:
REFERENCES 1. Lolis, E.M., Alber, T., Davenport, R.C., Rose, D., Hartman, F.C. and Petsko, G.A. (1990) Biochemistry 29, 6609-66182. Farber, G.K., Petsko, G.A. and Ringe, D. (1987) Prot. Eng. 1, 459-466 3. Neidhart, D.J., Howell, P.L., Petsko, G.A., Powers, V.M., Li, R., Kenyon, G.L. and Gerlt, J. (1991) Biochemistry 30, 9264-92734. Komives, E.A., Chang, L.C., Lolis, E., Tilton, R.F., Petsko, G.A. and Knowles, J.R. (1991) Biochemistry 30, 3011-30195. Farber, G.K., Glasfeld, A., Tiraby, G., Ringe, D. and Petsko, G.A. (1989) Biochemistry 28, 7289-7297 6. Gerhart-Mueller, E., Allen, K., Lavie, A., Ringe, D. and Petsko, G.A. (1992) in preparation 7. Bash, P.A., Field, M.J., Davenport, R.C., Petsko, G.A., Ringe, D. and Karplus, M. (1991) Biochemistry 30, 5826-5832 8. Gerlt, J.A., Kozarich, J.Y., Kenyon, G.L. and Gassman, P.G. (1991) J. Am. Chern. Soc. 113, 9667-9669 ACKNOYLEDGEMENT. Supported by grants from the U.S. National Institutes of Health.
Funding Information:
ACKNOWLEDGEMENTS Supported by NIH grant DK18865 to BMD. pTCPSD2 was a generous gift from G. Conner at the University of Miami.
PY - 1993
Y1 - 1993
N2 - The simplest chemical transformations in metabolism are the proton transfer reactions exemplified by certain isomerases and racemases. We have been studying three such enzymes to understand the structural features that lead to efficient proton transfer. All of these enzymes face the common problem of abstracting a hydrogen from a carbon acid of high pKa with an enzymic base of low pKa. We have used X-ray crystallography, site-directed mutagenesis, and molecular dynamics simulations to arrive at a set of principles for optimal catalysis of this simple reaction.
AB - The simplest chemical transformations in metabolism are the proton transfer reactions exemplified by certain isomerases and racemases. We have been studying three such enzymes to understand the structural features that lead to efficient proton transfer. All of these enzymes face the common problem of abstracting a hydrogen from a carbon acid of high pKa with an enzymic base of low pKa. We have used X-ray crystallography, site-directed mutagenesis, and molecular dynamics simulations to arrive at a set of principles for optimal catalysis of this simple reaction.
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U2 - 10.1093/protein/6.Supplement.37-a
DO - 10.1093/protein/6.Supplement.37-a
M3 - Article
AN - SCOPUS:84963062652
SN - 1741-0126
VL - 6
SP - 37
JO - Protein Engineering, Design and Selection
JF - Protein Engineering, Design and Selection
ER -