Electrostatic basis for enzyme catalysis

A Warshel, PK Sharma, M Kato, Y Xiang, H Liu… - Chemical …, 2006 - ACS Publications
Enzymatic reactions play a fundamentally important role in controlling and performing most
life processes. 1-3 Thus, understanding how enzymes work has both fundamental and …

Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites

A Warshel - Journal of Biological Chemistry, 1998 - ASBMB
Enzymatic reactions are involved in most biological processes. Thus, there is a major
practical and fundamental interest in finding out what makes enzymes so efficient. Many …

Sulfa and trimethoprim-like drugs–antimetabolites acting as carbonic anhydrase, dihydropteroate synthase and dihydrofolate reductase inhibitors

C Capasso, CT Supuran - Journal of enzyme inhibition and …, 2014 - Taylor & Francis
Recent advances in microbial genomics, synthetic organic chemistry and X-ray
crystallography provided opportunities to identify novel antibacterial targets for the …

Combinatorial and evolution‐based methods in the creation of enantioselective catalysts

MT Reetz - Angewandte Chemie International Edition, 2001 - Wiley Online Library
Combinatorial methods in the development of enantioselective homogeneous catalysts
constitute a new branch of catalysis research. The goal is to prepare libraries of potential …

DynaFit—a software package for enzymology

P Kuzmič - Methods in enzymology, 2009 - Elsevier
Since its original publication, the DynaFit software package [Kuzmič, P.(1996). Program
DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase. Anal …

The proton-translocating ATPase of Escherichia coli.

AE Senior - Annual review of biophysics and biophysical chemistry, 1990 - europepmc.org
The purpose of this review is to provide an up-to-date summary of E. coli proton-
translocating F1F0ATPase. From work on this enzyme, new insights have been gained in …

Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate. cntdot. NADP+ ternary complex. substrate binding and a model …

C Bystroff, SJ Oatley, J Kraut - Biochemistry, 1990 - ACS Publications
Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the
folate .cntdot. NADP+ ternary compl Page 1 Biochemistry 1990, 29, 3263-3277 3263 Crystal …

Enzymatic catalysts in organic synthesis

CH Wong - Science, 1989 - science.org
The synthetic value of enzymes is being increasingly recognized. With an understanding of
enzyme-catalyzed reactions and the techniques now available for the low-cost production …

Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines

MD Toney, JF Kirsch - Science, 1989 - science.org
A true Brønsted analysis of proton transfer in an enzyme mechanism is made possible by the
chemical rescue of an inactive mutant of aspartate aminotransferase, where the …

Coupling interactions of distal residues enhance dihydrofolate reductase catalysis: mutational effects on hydride transfer rates

PTR Rajagopalan, S Lutz, SJ Benkovic - Biochemistry, 2002 - ACS Publications
Recently, the participation in catalysis of residues spatially removed from the enzyme's
active site has received considerable attention. The influence of the distal Gly-121 residue …