Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Enzymes: Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.Biocatalysis: The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.Kinetics: The rate dynamics in chemical or physical systems.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Catalytic Domain: The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.Models, Chemical: Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Quantum Theory: The theory that the radiation and absorption of energy take place in definite quantities called quanta (E) which vary in size and are defined by the equation E=hv in which h is Planck's constant and v is the frequency of the radiation.Crystallography, X-Ray: The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Thermodynamics: A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)Enzyme Stability: The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Decarboxylation: The removal of a carboxyl group, usually in the form of carbon dioxide, from a chemical compound.Hydrogen: The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.Hydrogen Bonding: A low-energy attractive force between hydrogen and another element. It plays a major role in determining the properties of water, proteins, and other compounds.Histidine: An essential amino acid that is required for the production of HISTAMINE.Static Electricity: The accumulation of an electric charge on a objectTetrahydrofolate Dehydrogenase: An enzyme of the oxidoreductase class that catalyzes the reaction 7,8-dihyrofolate and NADPH to yield 5,6,7,8-tetrahydrofolate and NADPH+, producing reduced folate for amino acid metabolism, purine ring synthesis, and the formation of deoxythymidine monophosphate. Methotrexate and other folic acid antagonists used as chemotherapeutic drugs act by inhibiting this enzyme. (Dorland, 27th ed) EC 1.5.1.3.Structure-Activity Relationship: The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Oxidation-Reduction: A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).Molecular Conformation: The characteristic three-dimensional shape of a molecule.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Solvents: Liquids that dissolve other substances (solutes), generally solids, without any change in chemical composition, as, water containing sugar. (Grant & Hackh's Chemical Dictionary, 5th ed)Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Stereoisomerism: The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Molecular Structure: The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Spectrophotometry: The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.Amino Acid Substitution: The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.Protons: Stable elementary particles having the smallest known positive charge, found in the nuclei of all elements. The proton mass is less than that of a neutron. A proton is the nucleus of the light hydrogen atom, i.e., the hydrogen ion.Molecular Dynamics Simulation: A computer simulation developed to study the motion of molecules over a period of time.Protein Structure, Secondary: The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.NADP: Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)Oxidoreductases: The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)Cysteine: A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.Chromatography, High Pressure Liquid: Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Computer Simulation: Computer-based representation of physical systems and phenomena such as chemical processes.Nuclear Magnetic Resonance, Biomolecular: NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Magnetic Resonance Spectroscopy: Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).Water: A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Bacterial Proteins: Proteins found in any species of bacterium.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Oxygen: An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.Enzyme Activation: Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Molecular Weight: The sum of the weight of all the atoms in a molecule.RNA, Catalytic: RNA that has catalytic activity. The catalytic RNA sequence folds to form a complex surface that can function as an enzyme in reactions with itself and other molecules. It may function even in the absence of protein. There are numerous examples of RNA species that are acted upon by catalytic RNA, however the scope of this enzyme class is not limited to a particular type of substrate.Antibodies, Catalytic: Antibodies that can catalyze a wide variety of chemical reactions. They are characterized by high substrate specificity and share many mechanistic features with enzymes.Aspartic Acid: One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.Metals: Electropositive chemical elements characterized by ductility, malleability, luster, and conductance of heat and electricity. They can replace the hydrogen of an acid and form bases with hydroxyl radicals. (Grant & Hackh's Chemical Dictionary, 5th ed)Magnesium: A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Conserved Sequence: A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.Lysine: An essential amino acid. It is often added to animal feed.Proton-Translocating ATPases: Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.Nucleic Acid Conformation: The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.Manganese: A trace element with atomic symbol Mn, atomic number 25, and atomic weight 54.94. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver. (From AMA Drug Evaluations Annual 1992, p2035)Flavins: Derivatives of the dimethylisoalloxazine (7,8-dimethylbenzo[g]pteridine-2,4(3H,10H)-dione) skeleton. Flavin derivatives serve an electron transfer function as ENZYME COFACTORS in FLAVOPROTEINS.Arginine: An essential amino acid that is physiologically active in the L-form.Alkenes: Unsaturated hydrocarbons of the type Cn-H2n, indicated by the suffix -ene. (Grant & Hackh's Chemical Dictionary, 5th ed, p408)Protein Structure, Quaternary: The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).Cyclization: Changing an open-chain hydrocarbon to a closed ring. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Dimerization: The process by which two molecules of the same chemical composition form a condensation product or polymer.Flavin-Adenine Dinucleotide: A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)Diethyl Pyrocarbonate: Preservative for wines, soft drinks, and fruit juices and a gentle esterifying agent.Crystallization: The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)IminesNAD: A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)Asparagine: A non-essential amino acid that is involved in the metabolic control of cell functions in nerve and brain tissue. It is biosynthesized from ASPARTIC ACID and AMMONIA by asparagine synthetase. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)Phosphates: Inorganic salts of phosphoric acid.Circular Dichroism: A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Chemistry, Organic: The study of the structure, preparation, properties, and reactions of carbon compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Lewis Acids: Any chemical species which accepts an electron-pair from a LEWIS BASE in a chemical bonding reaction.Electron Spin Resonance Spectroscopy: A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.Heme: The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.Palladium: A chemical element having an atomic weight of 106.4, atomic number of 46, and the symbol Pd. It is a white, ductile metal resembling platinum, and following it in abundance and importance of applications. It is used in dentistry in the form of gold, silver, and copper alloys.Zinc: A metallic element of atomic number 30 and atomic weight 65.38. It is a necessary trace element in the diet, forming an essential part of many enzymes, and playing an important role in protein synthesis and in cell division. Zinc deficiency is associated with ANEMIA, short stature, HYPOGONADISM, impaired WOUND HEALING, and geophagia. It is known by the symbol Zn.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.CobamidesSpectrophotometry, Ultraviolet: Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Protein Folding: Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.Alanine: A non-essential amino acid that occurs in high levels in its free state in plasma. It is produced from pyruvate by transamination. It is involved in sugar and acid metabolism, increases IMMUNITY, and provides energy for muscle tissue, BRAIN, and the CENTRAL NERVOUS SYSTEM.Isomerism: The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)Electrons: Stable elementary particles having the smallest known negative charge, present in all elements; also called negatrons. Positively charged electrons are called positrons. The numbers, energies and arrangement of electrons around atomic nuclei determine the chemical identities of elements. Beams of electrons are called CATHODE RAYS.Cations, Divalent: Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis.Sulfhydryl Compounds: Compounds containing the -SH radical.Chorismate Mutase: An isomerase that catalyzes the conversion of chorismic acid to prephenic acid. EC 5.4.99.5.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
Warshel A (November 1978). "Energetics of enzyme catalysis". Proceedings of the National Academy of Sciences of the United ... The enzyme functions by attacking, hydrolyzing, and breaking glycosidic bonds in peptidoglycans. The enzyme can also break ... "Application of secondary alpha-deuterium kinetic isotope effects to studies of enzyme catalysis. Glycoside hydrolysis by ... "Application of secondary alpha-deuterium kinetic isotope effects to studies of enzyme catalysis. Glycoside hydrolysis by ...
... and enzyme catalysis; atmospheric and environmental chemistry; drug design; nanoparticle structure and energetics; and density ...
"Micromotors Powered by Enzyme Catalysis". Nano Letters. 15 (12): 8311-8315. doi:10.1021/acs.nanolett.5b03935. ISSN 1530-6984. ... "Substrate Catalysis Enhances Single Enzyme Diffusion". Journal of the American Chemical Society. 132 (7): 2110-2111. doi: ... Recent work has shown that enzyme molecules will also propel themselves. Further, it has been shown that they will ... The catalytic reactions of the enzymes direct the particles based on corresponding substrate gradients. There is a distinction ...
Since the 2000s, the general consensus has been that LBHBs are not used by enzymes to aid catalysis. However, in 2012, a low- ... Low-barrier hydrogen bonds have been proposed to be relevant to enzyme catalysis in two types of circumstance. Firstly, a low- ... "Electrostatic Basis for Enzyme Catalysis". Chemical Reviews. 106 (8): 3210-3235. doi:10.1021/cr0503106. PMID 16895325. Elias, ... Cleland, W. W.; Frey, P. A.; Gerlt, J. A. (2 October 1998). "The Low Barrier Hydrogen Bond in Enzymatic Catalysis". Journal of ...
Kohen, A.; Klinman, J. P. (1998). "Enzyme Catalysis: Beyond Classical Paradigms". Accounts of Chemical Research. 31 (7): 397- ... It has long been speculated that high efficiency of enzyme catalysis in proton or hydride ion transfer reactions could be due ... This can be explained for a mechanism of specific hydrogen-ion catalysis of a reactant R by H3O+ (or D3O+) . H3O+ + R = RH+ + ... Environment at the active site of an enzyme positions the donor and acceptor atom close to the optimal tunneling distance, ...
"Micromotors Powered by Enzyme Catalysis". Nano Letters. 15 (12): 8311-8315. doi:10.1021/acs.nanolett.5b03935. ISSN 1530-6984. ... This remains the only method of separating enzymes based on activity alone. Developing enzyme-driven nanomotors promises to ... It has since been shown that particles themselves will diffuse faster when coated with active enzyme molecules in a solution of ... At low Reynold's numbers, single molecule enzymes could act as autonomous nanomotors. Ayusman Sen and Samudra Sengupta ...
Meeuwissen, J.; Reek, J. N. H. (2010). "Supramolecular catalysis beyond enzyme mimics". Nat. Chem. 2 (8): 615-21. Bibcode: ... and catalysis. Hydrogen bonds are among the mostly used synthons in bottom-up approach to engineering molecular interactions in ...
Benkovic SJ, Hammes-Schiffer S (August 2003). "A perspective on enzyme catalysis". Science. 301 (5637): 1196-202. Bibcode: ... Dihydrofolate reductase catalyses the last step. Vitamin B3 in the form of NADPH is a necessary cofactor for both steps of the ... Also, polymorphisms in genes of enzymes involved in folate metabolism could be one reason for fertility complications in some ...
Knowles, J.R. (1991). "Enzyme catalysis: not different, just better". Nature. 350 (6314): 121-124. doi:10.1038/350121a0. PMID ... The active site of this enzyme is in the center of the barrel. A glutamic acid residue and a histidine are involved in the ... Catalysis of the reverse reaction proceeds analogously, forming the same enediol but with enediolate collapse from the oxygen ... TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as ...
"Substrate Catalysis Enhances Single-Enzyme Diffusion". Journal of the American Chemical Society. 132 (7): 2110-2111. doi: ... Self-propelled enzyme motors and synthetic nanomotors also exhibit clustering effects in the form of chemotaxis. Chemotaxis is ... Clustering also occurs in enzyme molecule diffusion. In all these experiments, the motion of particles takes place on a two- ... Clustering behavior in self-propelled particles and enzyme motors is discussed in great detail in sections on Collective ...
Kipp DR, Quinn CM, Fortin PD (2013). "Enzyme-dependent lysine deprotonation in EZH2 catalysis". Biochemistry. 52 (39): 6866-78 ... EZH2-mediated catalysis of H3K27me3 is associated with long term transcription repression. EZH2, as well as other Polycomb ... The drug blocks EZH2 activity by binding to the SET domain active site of the enzyme. EPZ005687 can also inhibit the Y641 and ... This is an issue because it means the methylation activity of the enzyme is not mediated by complex formation. In breast cancer ...
1 [Enzyme Catalysis, Vol. 1] (in Russian). Moscow University Press. Klyosov, A. A. (1984). Ферментативный катализ. Т. 2 [Enzyme ... enzyme catalysis, and industrial biochemistry. In 1989 Klyosov immigrated to the US. He spent most of his career developing ... 1980). Enzyme Engineering. N.Y.: Plenum Press. Klyosov, A. A.; Witczak, Z. J.; Platt, D., eds. (2006). Carbohydrate Drug Design ... He later helped found a company, and later joined it as CSO, that was founded to use enzymes to alter existing anticancer drugs ...
The enzymatic mechanism of influenza virus sialidase has been studied by Taylor et al., shown in Figure 1. The enzyme catalysis ... Neuraminidase enzymes are glycoside hydrolase enzymes that cleave the glycosidic linkages of neuraminic acids. Neuraminidase ... One is the lectin haemagglutinin protein with three relatively shallow sialic acid-binding sites and the other is enzyme ... the structure-based inhibitor design was applied to discover potent inhibitors of this enzyme. The unsaturated sialic acid (N- ...
... s also function as cofactors in enzyme catalysis. Folates are pterins that contain p-aminobenzoic acid connected to the ... the enzyme that controls the conversion of GTP to pterin, GTP cyclohydrolase I, is found in both prokaryotes and eukaryotes. ...
Enzyme catalysis Negative feedback Bhagavan, N. V (2002). Medical biochemistry. San Diego: Harcourt/Academic Press. ISBN 0-12- ... Brown ED, Vivas EI, Walsh CT, Kolter R (July 1995). "MurA (MurZ), the enzyme that catalyzes the first committed step in ... 3-deoxy-D-arabinose-heptulsonate 7-phosphate synthase catalyses the first committed step of the shikimate pathway responsible ...
Enzyme Abzyme Artificial enzyme Catalysis Wiseman A (1993). "Designer enzyme and cell applications in industry and in ... Like enzymes, they bind a transition state of a substrate in an active site, and like enzymes they generally obey Michaelis- ... The name synzyme is derived from synthetic enzyme. Current synzymes consist mainly of organic molecules tailored in such a way ... Antibodies can act as enzymes, then named abzymes, if they are selected against transition state analogues. Abzymes have a low ...
Chemistry portal Enzyme catalysis Hydrolase "ENZYME: 3.4.17.-". enzyme.expasy.org. Retrieved 2016-05-21. "AGBL1". www.genecards ... A metalloexopeptidase is a type of enzyme that acts as a metalloproteinase exopeptidase. These enzymes have a catalytic ... Using the Enzyme Commission number (EC number) system, metallocarboxypeptidases fall under EC 3.4.17. Examples of these ...
Fischer, J. D.; Holliday, G. L.; Thornton, J. M. (2010). "The CoFactor database: Organic cofactors in enzyme catalysis". ... Gutteridge, Alex (2005). Understanding the Relationship Between Enzyme Structure and Catalysis (PhD thesis). University of ... Martinez Cuesta, S; Furnham, N; Rahman, S. A.; Sillitoe, I; Thornton, J. M. (2014). "The evolution of enzyme function in the ... Martinez-Cuesta, Sergio (2014). The Chemistry and Evolution of Enzyme Function: Isomerases as a Case Study (PhD thesis). ...
"Protein motions and dynamic effects in enzyme catalysis". Physical Chemistry Chemical Physics. 46 (17): 30817-30827. doi: ... Allemann's work on hydrogen transfer catalysing enzymes including dihydrofolate reductase has led to deep new insights into the ... the pioneers in synthetic biology and has developed innovative applications such as the first generation of designer enzymes, ...
Kurumbail RG, Kiefer JR, Marnett LJ (December 2001). "Cyclooxygenase enzymes: catalysis and inhibition". Curr. Opin. Struct. ... Each monomer of the enzyme has a peroxidase and a PTGS (COX) active site. The PTGS (COX) enzymes catalyze the conversion of ... The tertiary and quaternary structures of PTGS1 (COX-1) and PTGS2 (COX-2) enzymes are almost identical. Each subunit has three ... PTGS1 (COX-1) and PTGS2 (COX-2) are bifunctional enzymes that carry out two consecutive chemical reactions in spatially ...
Decker H, Schweikardt T, Nillius D, Salzbrunn U, Jaenicke E, Tuczek F (August 2007). "Similar enzyme activation and catalysis ...
"Visualization of dioxygen bound to copper during enzyme catalysis". Science. 286 (5445): 1724-8. doi:10.1126/science.286.5445. ... In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen. This enzyme belongs ... The systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). This enzyme ... Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes ...
Drauz, Karlheinz (2010). Enzyme catalysis in organic synthesis : a comprehensive handbook (New ed.). Weinheim: Wiley-VCH. ISBN ... Biocatalysts and Enzyme Technology (2nd ed.). Weinheim: Wiley. ISBN 3-527-67200-1. Knackmuss, edited by Jim C. Spain, Joseph B ...
Active site Convergent evolution Divergent evolution Enzyme catalysis Enzyme superfamily Functional groups PA clan Protease ... The second stage of catalysis is the resolution of the acyl-enzyme intermediate by the attack of a second substrate. If this ... Catalytic triads perform covalent catalysis via an acyl-enzyme intermediate. If this intermediate is resolved by water, the ... the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes". ACS Catalysis. 5 (10): 6153-6176. doi:10.1021/ ...
2010). Enzyme catalysis in organic synthesis : a comprehensive handbook (New ed.). Weinheim: Wiley-VCH. ISBN 3-527-32547-6. M ...
They are labelled "Type I" if the defective gene is for an enzyme involved in the assembly or transfer of the Glc3Man9GlcNAc2- ...
They learned that the enzyme can exist in four different folded states, or conformers, that play an active role in the reaction ... These results will have consequences for enzyme engineering and the development of inhibitors. The study was published in ... University of Groningen scientists have observed the characteristics of a single enzyme inside a nanopore. ... "We chose this enzyme because it has been studied as a model system for enzyme dynamics for over 30 years, using all available ...
The mechanism of enzyme catalysis is similar in principle to other types of chemical catalysis. By providing an alternative ... Enzymes utilizing such cofactors include the PLP-dependent enzyme aspartate transaminase and the TPP-dependent enzyme pyruvate ... but is recycled such that a single enzyme performs many rounds of catalysis. The favored model for the enzyme-substrate ... Play media Enzyme catalysis is the increase in the rate of a chemical reaction by the active site of a protein. The protein ...
Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions ... Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunnelling and dynamical ... Computer simulations of enzyme catalysis: Finding out what has been optimized by evolution ... Structure and Catalysis of Acylaminoacyl Peptidase: CLOSED AND OPEN SUBUNITS OF A DIMER OLIGOPEPTIDASE ...
... Åqvist, Johan Uppsala University, Disciplinary Domain of Science and Technology, Biology, ... no real consensus has been reached regarding the origin of such large entropic contributions to enzyme catalysis. Another ... These cold-adapted enzymes invariably show a more negative entropy and a lower enthalpy of activation than their mesophilic ... It turns out that the large entropy contributions to catalysis in these cases can now be rationalized by our computational ...
... including the enzyme structure, their kinetic and chemical mechanisms and the experimental aspects of enzymology. ... ENZYMES: Catalysis, Kinetics and Mechanisms. Authors. * N.S. Punekar Copyright. 2018. Publisher. Springer Singapore. Copyright ... and also highlights the synergy between enzyme structure and mechanism. Designed for self-study, it explains how to plan enzyme ... The book is divided into five major sections: 1] Introduction to enzymes, 2] Practical aspects, 3] Kinetic Mechanisms, 4] ...
The Enzyme Catalysis Process. Book Subtitle. Energetics, Mechanism and Dynamics. Editors. * A. Cooper ... It was not our intention at this meeting to present a complete up-to-the-minute review of current research in enzyme catalysis ... The Enzyme Catalysis Process. Energetics, Mechanism and Dynamics. Editors: Cooper, A. (Ed.) ... The Fluorescence Properties of Aromatic Amino Acids: Their Role in the Understanding of Enzyme Structure and Dynamics ...
Browse our large selection of Enzyme Catalysis Kits & Biology at Nasco. You will find a unique blend of products for Arts & ...
Evolutionary drivers of thermoadaptation in enzyme catalysis Message Subject. (Your Name) has forwarded a page to you from ... Evolutionary drivers of thermoadaptation in enzyme catalysis. By Vy Nguyen, Christopher Wilson, Marc Hoemberger, John B. ... Evolutionary drivers of thermoadaptation in enzyme catalysis. By Vy Nguyen, Christopher Wilson, Marc Hoemberger, John B. ...
Lets explore what enzymes are, and how they can affect a reaction. The most important affect you need to know is its ability ...
Lets explore what enzymes are, and how they can affect a reaction. The most important affect you need to know is its ability ... So first Ill mention acid/base catalysis, which happens when enzymes act like either acids or bases. Now, remember that acids ... And we need enzymes because enzymes make all of these reactions go much faster. And lets look at this idea little more deeply ... Our next catalytic strategy is covalent catalysis, which happens when enzymes form a covalent bond with another molecule, ...
... Problem 9: Kinetics of an enzyme reaction with a non-competitive inhibitor. Which of ... non-competitive inhibitors bind to an enzyme at a site different than the active site)? ... the following graphs shows the results of reaction rate vs substrate concentration for an non-allosteric enzyme in the absence ...
The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes.. Banerjee R1, Ragsdale SW. ... Over the past decade our understanding of the reaction mechanisms of B12 enzymes has been greatly enhanced by the availability ... Different chemical aspects of the cofactor are exploited during catalysis by the isomerases and the methyltransferases. Thus, ... The reaction mechanism of the dehalogenases, the most recently discovered class of B12 enzymes, is poorly understood. ...
The role of dimer asymmetry and protomer dynamics in enzyme catalysis. By Tae Hun Kim, Pedram Mehrabi, Zhong Ren, Adnan Sljoka ... The role of dimer asymmetry and protomer dynamics in enzyme catalysis. By Tae Hun Kim, Pedram Mehrabi, Zhong Ren, Adnan Sljoka ... The role of dimer asymmetry and protomer dynamics in enzyme catalysis Message Subject. (Your Name) has forwarded a page to you ... An enzyme homodimer engages both subunits-one binds substrate in its active site; the other allosterically enhances catalysis. ...
Enzyme catalysis is the catalysis of chemical reactions by specialized proteins, enzymes. Catalysis of biochemical reactions in ... The mechanism of enzyme catalysis is similar in principle to other types of chemical catalysis. By providing an alternative ... Catalysis by induced fit. File:Enzyme catalysis uniform+differential binding.png The different mechanisms of substrate binding ... File:Enzyme catalysis delta delta G.png Stabilization of the transition state by an enzyme. ...
2010) At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis? Proteins 78:1339-1375. ... Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions. ... Thus, moving along the enzyme coordinate is a part of the free-energy landscape, and it does not explain any catalysis ( ... 2007) A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450:913-916. ...
... The structure is the smallest known biological reaction chamber ... Enzymes that catalyze multiple reactions from a reactant to a product often have evolved a way to get intermediates from one ... "Its not simply three enzymes fused to each other," Erb says. "They are fused to each other in a way that they form a ... The enzyme undergoes synchronized conformational changes that let substrates and products in and out of the reaction chamber. ...
Oxidizing Enzymes into Multi-Enzyme Biotransformation Processes. The Role of Host-Intrinsic Enzyme Activities in Recombinant ... Multi-Step Enzyme Catalysis: Biotransformations and Chemoenzymatic Synthesis. Eduardo Garcia-Junceda (Editor) ... Asymmetric Transformations by Couples Enzymes and Metal Catalysis. Engineering Novel Biosynthetic Pathways to Produce New ... His research interests concentrate on molecular biology applied to organic synthesis and enzyme catalysis.. ...
Enzyme dynamics, conformations and catalysis. Add to your list(s) Download to your calendar using vCal ... University of Cambridge , Talks.cam , Centre for Molecular Science Informatics , Enzyme dynamics, conformations and catalysis ...
How do enzymes affect forward and reverse reaction rate & what does this means?. ... Describe the energetic of catalysis in simplest terms? 3. ... Enzyme - rate enhancement and energetic of catalysis. Add. ... brainmass.com/biology/enzyme-catalysts-and-reactions/enzyme-rate-enhancement-energetic-catalysis-101007 Solution Preview. 1. ... 2. Describe the energetic of catalysis in simplest terms?. 3. How do enzymes affect forward and reverse reaction rate & what ...
... an enzyme necessary for nucleotide biosynthesis and a classical drug target. ... a team of researchers unequivocally mapped the active site of the enzyme dihydrofolate reductase (DHFR), ... Seeing hydrogen atoms to unveil enzyme catalysis. (Nanowerk News) Enzymes are catalysts that speed up chemical reactions in ... We were able to detect protonation states at select sites in the enzyme to resolve mechanisms concerning acid-base catalysis, ...
Enzyme Catalysis 8-Station Kit with 8 Burets (with perishable). Item # 746432P Online Only Exclusive *bvseo_sdk, java_sdk, ... Enzyme Catalysis 8-Station Replacement Set (with prepaid coupon) Item #746435 $49.55 ... Observation and study of enzyme-mediated reactions *Observe the action of an enzyme ... Monitor the effect of heat on enzyme activity. Designed to match traditional AP® Biology Lab 2. Easy-to-use kit format ...
Single nanoparticles and enzymes catalysis I. Using new electrochemical techniques it is now possible to characterize ... We seek to investigate the mechanism of single enzyme catalysis by state of the art electrochemical techniques, which includes ... II. Enzymes are typically natural efficient catalysts. The macroscopic behavior of enzymes has been attracted the scientific ... Because of the flexibility and the dynamical structure of enzymes, each enzyme may have its own catalytic rate and this ...
... investigate the rates of enzyme catalyzed reactions by observing the decomposition of hydrogen peroxide by catalase. Refill is ... With the Enzyme Catalysis Laboratory Kit for Classic AP* Biology Lab 2, ... With the Enzyme Catalysis Laboratory Kit for Classic AP* Biology Lab 2, investigate the rates of enzyme catalyzed reactions by ... Enzyme Catalysis-AP* Biology Lab 2, 3 Groups. By: The Flinn Staff ... Enzyme Catalysis-AP* Biology Lab 2-Refill Kit. Item No. FB1831 ...
... Problem 4: An energy barrier separating reactions and products in a chemical ...
  • These effects have led to most proteins using the differential binding mechanism to reduce the energy of activation, so most substrates have high affinity for the enzyme while in the transition state. (wikipedia.org)
  • The use of gaseous substrates and products provides an experimental system in which the hydration of the enzyme can be easily controlled, but which is not limited by diffusion. (royalsocietypublishing.org)
  • It is amazing, however, how much information about the mechanism of enzyme action can be gained even if all you have is a blender, a stopwatch, an impure enzyme, and a few substrates and inhibiting reagents. (golifescience.com)
  • For lysozyme, we will study the structural features of the enzyme and substrates along with the mechanism for cleavage of glycosidic links in bacterial peptidoglycan cell walls. (golifescience.com)
  • In the cell, enzymes acting on similar pathways are often located next to one another so that substrates don't have to diffuse away from one enzyme to the next-a mechanism that allows the enzymes to be more efficient than the theoretical limit. (golifescience.com)
  • Background: Enzymes are proteins with specific 3D conformations, or shapes, which allow them to interact with specifically shaped substrates in an active site region. (bartleby.com)
  • Paul Andersen starts with a brief description of enzymes and substrates. (bibliotekaniedrzwica.eu)
  • COX-2 is naturally inhibited by Calcitriol (the active form of Vitamin D). Both the peroxidase and PTGS activities are inactivated during catalysis by mechanism-based, first-order processes, which means that PGHS-2 peroxidase or PTGS activities fall to zero within 1-2 minutes, even in the presence of sufficient substrates. (wikipedia.org)
  • In recent years, it has become clear that enzymes are not rigid structures, but that the folded proteins exist as an ensemble of conformations in equilibrium around an energetically stable ground state. (phys.org)
  • Professor Mulholland said: "As our research indicates that this type of interaction is likely to be important in other enzymes, it could ultimately help in the design of new proteins with applications in medicine and bioengineering. (phys.org)
  • Here we report the discovery of an enzyme in a Golgi-enriched fraction that catalyses guanine nucleotide (GDP-GTP) exchange on ARF-1 protein, and which is inhibited by brefeldin A. We suggest that activation of ARF proteins for membrane localization by compartmentalized exchange enzymes is in general the first committed step in membrane transformation pathways. (nih.gov)
  • OxDc is a member of the cupin superfamily, which comprises a wide variety of proteins and enzymes with great sequence and functional diversity. (bu.edu)
  • Proteins however exhibit a large degree of motion over a broad range of timescales and magnitudes and this is defined thermodynamically by the enzyme free energy landscape (FEL). (bath.ac.uk)
  • Enzymes are proteins produced by living cells. (nation2.com)
  • Snake venoms are cocktails of enzymes and non-enzymatic proteins used for both the immobilization and digestion of prey. (tailieu.vn)
  • Enzymes may be considered as one of the most of import proteins of the human organic structure. (graduateway.com)
  • Enzymes are by and large big proteins that consist of several hundred aminic acids, and frequently incorporate a non-proteinaceous group otherwise known as a prosthetic group of which is of import in the existent contact action. (graduateway.com)
  • Most enzymes are proteins(such as pepsin enzyme ) whose molecular weight ranges from about 10,000 to more than 1,000,000. (hopetribune.com)
  • Water present in the organic solvent at a concentration of about 0.03% to about 2.5% is sufficient to enhance the rate of catalysis and stabilize the enzyme without substantially increasing the rate of hydrolysis when compared to the anhydrous enzyme. (uiowa.edu)
  • When the enzyme concentration was increased from 0.2-2.0, enzyme activity and hydrolysis values increased from 31.0% to 84.0% and from 69.0% to 85.0%, respectively. (bartleby.com)
  • The optimum enzyme concentration for hydrolysis was achieved as 1.2 g/L. At concentrations of past 1.2 g/L, starch hydrolysis rate did not change significantly (Dilek, 2004). (bartleby.com)
  • The Glu35 reacts with water to form hydroxyl ion, a stronger nucleophile than water, which then attacks the glycosyl enzyme intermediate, to give the product of hydrolysis and leaving the enzyme unchanged. (wikipedia.org)
  • The thiol analog of galactose, 6-Thio-Me-Gal, is also turned over by the enzyme, albeit at a much reduced rate, indicating that the energetics of turnover is changed significantly. (elsevier.com)
  • Chapters 1 and 2 of this dissertation analyzes the structure and function of the Mn-dependent enzyme oxalate decarboxylase (OxDc) and Chapter 2 presents a bioinformatic analysis of the cupin superfamily that provides the structural scaffold of the decarboxylase. (bu.edu)
  • Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF. (nih.gov)
  • They put to rest the claims that substances like charcoal caused inhibition of the enzymes (due to adsorption) and established that adsorption had no role in the decreased activity of the enzymes. (rsc.org)
  • His research interests concentrate on molecular biology applied to organic synthesis and enzyme catalysis. (wiley.com)
  • Moreover, the surge in applications of enzymes in various industries such as paper processing, biofuels, contact lens cleaners, rubber processing, biological detergents, and molecular biology will contribute to expansion in the global enzymes market in the projected periods. (aarkstore.com)
  • Gadi Rothenberg is Professor at the Van `t Hoff Institute for Molecular Sciences at the University of Amsterdam, where he teaches courses on catalysis, thermodynamics and scientific writing. (wiley.com)
  • download molecular aspects of enzyme catalysis to flee the smartphone. (avjetrouting.com)
  • New York: I. Web LinkRegression Discontinuity and the Price Effects of Stock Market download molecular aspects of enzyme catalysis Chang, Yen-cheng. (avjetrouting.com)
  • In download molecular aspects of enzyme to seem out of this today read connect your streaming website 1d8+1d8 to buy to the athletic or original bringing. (avjetrouting.com)
  • Galactose oxidase, a mononuclear copper enzyme, oxidizes primary alcohols to aldehydes using molecular oxygen. (elsevier.com)
  • We start by reproducing the trend in the measured change in catalysis upon mutations (which was assumed to arise as a result of a "dynamical knockout" caused by the mutations). (pnas.org)
  • It was then argued that the observed changes in the rate of the chemical step upon mutations that appear to prevent the flexibility of the active-site residues could be interpreted as evidence for a dynamical coupling to catalysis. (pnas.org)
  • Because of the flexibility and the dynamical structure of enzymes, each enzyme may have its own catalytic rate and this catalytic rate may not be constant over time (static and dynamic disorder). (ucsb.edu)
  • This paper will also consider briefly the dynamical effects and conclude that such effects do not contribute in a significant way to enzyme catalysis. (royalsocietypublishing.org)
  • Instead, it is argued by some workers that dynamical effects (such as "vibrational gating") and quantum-mechanical tunneling may be contributing to catalysis. (edu.au)
  • Meggers, E. Asymmetric catalysis activated by visible light. (nature.com)
  • Both this ligand set and the anomeric shape-tuning concept are expected to find broad application, given the value of chiral 1,2-diamines and salens constructed from these in asymmetric catalysis. (sciencemag.org)
  • The first comprehensive coverage of this unique and interdisciplinary field provides a complete overview, covering such topics as chemoenzymatic synthesis, microbial production of DNA building blocks, asymmetric transformations by coupled enzymes and much more. (wiley.com)
  • Basic concept of phase-transfer catalysis (PTC), its field of applications and specific features as the most general, efficient, and environment-friendly green methodology of organic synthesis, particularly for industrial processes, is discussed. (degruyter.com)
  • In heterogeneous catalysis , the diffusion of reagents to the surface and diffusion of products from the surface can be rate determining. (wikipedia.org)
  • Jointly organized by Italy's Research Council and Palermo's University, the 6th edition of the " FineCat - Symposium on heterogeneous catalysis for fine chemicals " was held in Sicily's Royal Palace in Palermo on April 5th . (rsc.org)
  • Professor Raed Abu-Reziq , of the Hebrew University of Jerusalem, Israel, presented the results of his team concerning the development of new nanostructured materials, nano- and microreactors as platforms for heterogeneous catalysis. (rsc.org)
  • It focuses on the synchrony between the two broad mechanistic facets of enzymology: the chemical and the kinetic, and also highlights the synergy between enzyme structure and mechanism. (springer.com)
  • abstract = "Our understanding of how enzymes work is colored by static structure depictions where the enzyme scaffold is presented as either immobile, or in equilibrium between well-defined static conformations. (bath.ac.uk)
  • University of Groningen scientists have observed the characteristics of a single enzyme inside a nanopore. (phys.org)
  • Illustration of the funnel-shaped nanopore (blue) surrounded by the artificial membrane (yellow), with a single enzyme (red/white/blue) trapped inside the pore. (phys.org)
  • This means that you can only see them in these kinds of long-lasting single enzyme studies. (phys.org)
  • However, a clear knowledge on the catalytic activity at a single enzyme level is still missing. (ucsb.edu)
  • We seek to investigate the mechanism of single enzyme catalysis by state of the art electrochemical techniques, which includes low noise electronic systems that is sufficient enough to enable detecting electronic signal above the noise level, arising from a single enzyme. (ucsb.edu)
  • Enzyme catalysis in organic solutions containing water" by Jonathan S. Dordick, Vikram M. Paradkar et al. (uiowa.edu)
  • Already used for the production of bulk chemicals, gold catalysis is poised to be introduced in the production of the basic ingredients of a wide variety of valued added products ranging from pharmaceuticals through liquid crystals and organic light emitting diodes (OLED) for computer, TV and mobile phone screens. (rsc.org)
  • Enzyme productiveness like many other things our organic structures tend to change based on outside factors. (graduateway.com)
  • The human organic structure is possibly the greatest trial of enzyme adaptability. (graduateway.com)
  • To our knowledge, this method represents the first example of photo-induced enzyme promiscuity, and highlights the potential for accessing new reactivity from existing enzymes simply by using the excited states of common biological co-factors. (nature.com)