Listar por tema "enzyme catalysis"
Mostrando ítems 1-11 de 11
-
Accelerated Polyethylene Terephthalate (PET) Enzymatic Degradation by Room Temperature Alkali Pre-treatment for Reduced Polymer Crystallinity
Wiley (2022-11-07)Polyethylene terephthalate (PET) is the most widely employed plastic for single-use applications. The use of enzymes isolated from microorganisms, such as PETase with the capacity to hydrolyze PET into its monomers, ... -
Do Dynamic Effects Play a Significant Role in Enzymatic Catalysis? A Theoretical Analysis of Formate Dehydrogenase
Wiley-VCH (2010)A theoretical study of the protein dynamic effects on the hydride transfer between the formate anion and nicotinamide adenine dinucleotide (NAD+), catalyzed by formate dehydrogenase (FDH), is presented in this paper. The ... -
Elucidating the Catalytic Reaction Mechanism of Orotate Phosphoribosyltransferase by Means of X‑ray Crystallography and Computational Simulations
American Chemical Society (2020-01-02)Orotate phosphoribosyltransferase (OPRTase) catalyzes the reaction between the ribose donor α-d-5-phosphoribosyl-1-pyrophosphate (PRPP) and orotate (OA) in the presence of Mg2+ ion to obtain pyrophosphate and pyrimidine ... -
Exploring the Origin of Amidase Substrate Promiscuity in CALB by a Computational Approach
American Chemical Society (2020)Enzyme promiscuity attracts the interest of the industrial and academic sectors because of its application in the design of biocatalysts. The amidase activity of Candida antarctica lipase B (CALB) on two different substrates ... -
Insights on the Origin of Catalysis on Glycine N-Methyltransferase from Computational Modeling
American Chemical Society (2018-02)The origin of enzyme catalysis remains a question of debate despite much intense study. We report a QM/MM theoretical study of the SN2 methyl transfer reaction catalyzed by a glycine N-methyltransferase (GNMT) and three ... -
Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State
Wiley (2018-03-12)The origin of substrate preference in promiscuous enzymes was investigated by enzyme isotope labelling of the alcohol dehydrogenase from Geobacillus stearothermophilus (BsADH). At physiological temperature, protein dynamic ... -
Minimization of dynamic effects in the evolution of dihydrofolate reductase
Royal Society of Chemistry (2016)Protein isotope labeling is a powerful technique to probe functionally important motions in enzyme catalysis and can be applied to investigate the conformational dynamics of proteins. Previous investigations have indicated ... -
Origin of Enzymatic Kinetic Isotope Effects in Human Purine Nucleoside Phosphorylase
American Chemical Society (2017)Here we report a study of the effect of heavy isotope labeling on the reaction catalyzed by human purine nucleoside phosphorylase (hPNP) to elucidate the origin of its catalytic effect and of the enzymatic kinetic isotope ... -
QM/MM Study of the Enzymatic Biodegradation Mechanism of Polyethylene Terephthalate
American Chemical Society (2021-06-04)The environmental problems derived from the generalized plastic consumption and disposal could find a friendly solution in enzymatic biodegradation. Recently, two hydrolases from Ideonella sakaiensis 201-F6 and the ... -
Revealing the Origin of the Efficiency of the De Novo Designed Kemp Eliminase HG-3.17 by Comparison with the Former Developed HG-3
Wiley (2017-05)The design of new biocatalysts is a goal in biotechnology to improve the rate, selectivity and environmental impact of industrial chemical processes. In this regard, the use of computational techniques has provided valuable ... -
Unraveling the Reaction Mechanism of Enzymatic C5-Cytosine Methylation of DNA. A Combined Molecular Dynamics and QM/MM Study of Wild Type and Gln119 Variant
American Chemical Society (2016)M.HhaI is a DNA methyltransferase from Haemophilus hemolyticus that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (SAM) to the C5 position of a cytosine. This enzyme is a paradigmatic model for C5 ...