The dynamical nature of enzymatic catalysis
R Callender, RB Dyer - Accounts of chemical research, 2015 - ACS Publications
Conspectus As is well-known, enzymes are proteins designed to accelerate specific life
essential chemical reactions by many orders of magnitude. A folded protein is a highly …
essential chemical reactions by many orders of magnitude. A folded protein is a highly …
Dynamic dissociating homo-oligomers and the control of protein function
T Selwood, EK Jaffe - Archives of Biochemistry and Biophysics, 2012 - Elsevier
Homo-oligomeric protein assemblies are known to participate in dynamic association/
disassociation equilibria under native conditions, thus creating an equilibrium of assembly …
disassociation equilibria under native conditions, thus creating an equilibrium of assembly …
[图书][B] Kinetics for the life sciences: receptors, transmitters and catalysts
H Gutfreund - 1995 - books.google.com
The aim of the book is to introduce the reader to the kinetic analysis of a wide range of
biological processes at the molecular level. It is intended to show that the same approach …
biological processes at the molecular level. It is intended to show that the same approach …
Site-directed mutagenesis reveals role of mobile arginine residue in lactate dehydrogenase catalysis
AR Clarke, DB Wigley, WN Chia, D Barstow, T Atkinson… - Nature, 1986 - nature.com
The binding of substrates to lactate dehydrogenases induces a marked rearrangement of
the protein structure in which a 'loop'of polypeptide (residues 98–110) closes over the active …
the protein structure in which a 'loop'of polypeptide (residues 98–110) closes over the active …
Design and synthesis of new enzymes based on the lactate dehydrogenase framework
CR Dunn, HM Wilks, DJ Halsall… - … of the Royal …, 1991 - royalsocietypublishing.org
Analysis of the mechanism and structure of lactate dehydrogenases is summarized in a map
of the catalytic pathway. Chemical probes, single tryptophan residues inserted at specific …
of the catalytic pathway. Chemical probes, single tryptophan residues inserted at specific …
Stochastic roadmap simulation: An efficient representation and algorithm for analyzing molecular motion
Classic techniques for simulating molecular motion, such as the Monte Carlo and molecular
dynamics methods, generate individual motion pathways one at a time and spend most of …
dynamics methods, generate individual motion pathways one at a time and spend most of …
Deciphering evolutionary trajectories of lactate dehydrogenases provides new insights into allostery
AY Robin, C Brochier-Armanet… - Molecular Biology …, 2023 - academic.oup.com
Abstract Lactate dehydrogenase (LDH, EC. 1.1. 127) is an important enzyme engaged in the
anaerobic metabolism of cells, catalyzing the conversion of pyruvate to lactate and NADH to …
anaerobic metabolism of cells, catalyzing the conversion of pyruvate to lactate and NADH to …
An investigation of the contribution made by the carboxylate group of an active site histidine-aspartate couple to binding and catalysis in lactate dehydrogenase
AR Clarke, HM Wilks, DA Barstow, T Atkinson… - Biochemistry, 1988 - ACS Publications
Department of Biochemistry, University of Bristol Medical School, University Walk, Bristol
BS8 1TD, UK, and Microbial Technology Laboratory, PHLS Centre for Applied Microbiology …
BS8 1TD, UK, and Microbial Technology Laboratory, PHLS Centre for Applied Microbiology …
Relaxation kinetics of cytochrome P450 reductase: internal electron transfer is limited by conformational change and regulated by coenzyme binding
A Gutierrez, M Paine, CR Wolf, NS Scrutton… - Biochemistry, 2002 - ACS Publications
The kinetics of internal electron transfer in human cytochrome P450 reductase have been
studied using temperature-jump relaxation spectroscopy. Temperature perturbation of CPR …
studied using temperature-jump relaxation spectroscopy. Temperature perturbation of CPR …
The approach to the Michaelis complex in lactate dehydrogenase: the substrate binding pathway
S McClendon, N Zhadin, R Callender - Biophysical journal, 2005 - cell.com
We examine here the dynamics of forming the Michaelis complex of the enzyme lactate
dehydrogenase by characterizing the binding kinetics and thermodynamics of oxamate (a …
dehydrogenase by characterizing the binding kinetics and thermodynamics of oxamate (a …