Results 11 to 20 of about 2,040,864 (360)

Fumarate analogs act as allosteric inhibitors of the human mitochondrial NAD(P)+-dependent malic enzyme. [PDF]

PLoS ONE, 2014
Human mitochondrial NAD(P)+-dependent malic enzyme (m-NAD(P)-ME) is allosterically activated by the four-carbon trans dicarboxylic acid, fumarate. Previous studies have suggested that the dicarboxylic acid in a trans conformation around the carbon-carbon
Ju-Yi Hsieh, Jyung-Hurng Liu, Pai-Chun Yang, Chi-Li Lin, Guang-Yaw Liu, Hui-Chih Hung   +5 more
doaj   +17 more sources

Mechanistic Insights into the Mechanism of Allosteric Inhibition of Ubiquitin-Specific Protease 7 (USP7) [PDF]

Biomolecules
Ubiquitin-specific protease 7 (USP7), a deubiquitinase enzyme responsible for removing ubiquitin (Ub) from target proteins, plays a crucial role in oncogenic pathways and has been implicated in various human diseases.
Xuebin Wang, Ning Liu, Nuan Li, Shaoyong Lu, Zongtao Chai   +4 more
doaj   +2 more sources

A Novel Fold Revealed by Mycobacterium tuberculosis NAD Kinase, a Key Allosteric Enzyme in NADP Biosynthesis [PDF]

Journal of Biological Chemistry, 2004
NAD kinase catalyzes the magnesium-dependent phosphorylation of NAD, representing the sole source of freshly synthesized NADP in all organisms. The enzyme is essential for the growth of the deadly multidrug-resistant pathogen Mycobacterium tuberculosis ...
Silvia Garavaglia, Nadia Raffaelli, Lucia Finaurini, Giulio Magni, Menico Rizzi   +4 more
openalex   +2 more sources

Substrate-Based Allosteric Regulation of a Homodimeric Enzyme.

Journal of the American Chemical Society, 2019
Many enzymes operate through half-of-the sites reactivity wherein a single protomer is catalytically engaged at one time. In the case of the homodimeric enzyme, fluoroacetate dehalogenase, substrate binding triggers closing of a regulatory cap domain in ...
P. Mehrabi, Christopher Di Pietrantonio, T. H. Kim, Adnan Sljoka, Keith Taverner, Christopher E. Ing, Natasha Kruglyak, R. Pomès, E. F. Pai, R. S. Prosser   +9 more
semanticscholar   +5 more sources

Molecular Synchronization Waves in Arrays of Allosterically Regulated Enzymes [PDF]

Physical Review Letters, 2007
Spatiotemporal pattern formation in a product-activated enzymic reaction at high enzyme concentrations is investigated. Stochastic simulations show that catalytic turnover cycles of individual enzymes can become coherent and that complex wave patterns of molecular synchronization can develop. The analysis based on the mean-field approximation indicates
Vanessa Casagrande, Yuichi Togashi, Alexander S. Mikhailov   +2 more
openalex   +7 more sources

Allosteric Binding Sites of the SARS-CoV-2 Main Protease: Potential Targets for Broad-Spectrum Anti-Coronavirus Agents

Drug Design, Development and Therapy, 2022
Lara Alzyoud,1 Mohammad A Ghattas,1,2 Noor Atatreh1,2 1College of Pharmacy, Al Ain University, Abu Dhabi, United Arab Emirates; 2AAU Health and Biomedical Research Center, Al Ain University, Abu Dhabi, United Arab EmiratesCorrespondence: Mohammad A ...
Alzyoud L, Ghattas MA, Atatreh N
doaj   +2 more sources

Mixed and non-competitive enzyme inhibition: underlying mechanisms and mechanistic irrelevance of the formal two-site model

Journal of Enzyme Inhibition and Medicinal Chemistry, 2023
The formal mechanism of linear mixed and non-competitive enzyme inhibition implies the binding of inhibitors to both the active site of the free enzyme in competition with the substrate, and to an allosteric site on the enzyme-substrate complex. However,
Alessandro Pesaresi
doaj   +2 more sources

Dissecting the Allosteric Fine-Tuning of Enzyme Catalysis

JACS Au
Fully understanding the mechanism of allosteric regulation in biomolecules requires separating and examining all of the involved factors. In enzyme catalysis, allosteric effector binding shifts the structure and dynamics of the active site, leading to modified energetic (e.g., energy barrier) and dynamical (e.g., diffusion coefficient) factors ...
Xin-Qiu Yao, Donald Hamelberg
doaj   +3 more sources

THE BINDING OF NICOTINAMIDE-ADENINE DINUCLEOTIDE TO YEAST D-GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE: TEMPERATURE-JUMP RELAXATION STUDIES ON THE MECHANISM OF AN ALLOSTERIC ENZYME

Proceedings of the National Academy of Sciences of the United States of America, 1966
Kasper Kirschner, Manfred Eigen, Robert Bittman, B. VOIGT   +3 more
openalex   +2 more sources

Coevolution-based prediction of key allosteric residues for protein function regulation

eLife, 2023
Allostery is fundamental to many biological processes. Due to the distant regulation nature, how allosteric mutations, modifications, and effector binding impact protein function is difficult to forecast.
Juan Xie, Weilin Zhang, Xiaolei Zhu, Minghua Deng, Luhua Lai   +4 more
doaj   +1 more source