28 relations: Acetylcholinesterase, Active site, Beta-lactamase, Carbonic anhydrase, Catalase, Catalysis, Cytochrome c peroxidase, Diffusion, Diffusion-controlled reaction, Enzyme, Enzyme catalysis, Enzyme kinetics, Fitness (biology), Fitness landscape, Fumarase, Gordon Hammes, Kuo-Chen Chou, Manfred Eigen, Mutation, Natural selection, Product (chemistry), Protein engineering, Quantum tunnelling, Rate-determining step, Specificity constant, Substrate (chemistry), Superoxide dismutase, Triosephosphate isomerase.
Acetylcholinesterase
Acetylcholinesterase, encoded by HGNC gene ACHE; EC 3.1.1.7) is the primary cholinesterase in the body. It is an enzyme that catalyzes the breakdown of acetylcholine and of some other choline esters that function as neurotransmitters. AChE is found at mainly neuromuscular junctions and in chemical synapses of the cholinergic type, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides.
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Active site
In biology, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction.
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Beta-lactamase
Beta-lactamases are enzymes produced by bacteria that provide multi-resistance to β-lactam antibiotics such as penicillins, cephalosporins, cephamycins, and carbapenems (ertapenem), although carbapenems are relatively resistant to beta-lactamase.
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Carbonic anhydrase
The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the interconversion between carbon dioxide and water and the dissociated ions of carbonic acid (i.e. bicarbonate and protons).
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Catalase
Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals).
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Catalysis
Catalysis is the increase in the rate of a chemical reaction due to the participation of an additional substance called a catalysthttp://goldbook.iupac.org/C00876.html, which is not consumed in the catalyzed reaction and can continue to act repeatedly.
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Cytochrome c peroxidase
Cytochrome c peroxidase, or CCP, is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing equivalents from cytochrome ''c'' and reduces hydrogen peroxide to water: CCP can be derived from aerobically grown yeast strains and can be isolated in both native and recombinant forms with high yield from Saccharomyces cerevisae. The enzyme’s primary function is to eliminate toxic radical molecules produced by the cell which are harmful to biological systems.
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Diffusion
Diffusion is the net movement of molecules or atoms from a region of high concentration (or high chemical potential) to a region of low concentration (or low chemical potential) as a result of random motion of the molecules or atoms.
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Diffusion-controlled reaction
Diffusion-controlled (or diffusion-limited) reactions are reactions that occur so quickly that the reaction rate is the rate of transport of the reactants through the reaction medium (usually a solution).
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Enzyme
Enzymes are macromolecular biological catalysts.
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Enzyme catalysis
Enzyme catalysis is the increase in the rate of a chemical reaction by the active site of a protein.
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Enzyme kinetics
Enzyme kinetics is the study of the chemical reactions that are catalysed by enzymes.
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Fitness (biology)
Fitness (often denoted w or ω in population genetics models) is the quantitative representation of natural and sexual selection within evolutionary biology.
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Fitness landscape
In evolutionary biology, fitness landscapes or adaptive landscapes (types of evolutionary landscapes) are used to visualize the relationship between genotypes and reproductive success.
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Fumarase
Fumarase (or fumarate hydratase) is an enzyme that catalyzes the reversible hydration/dehydration of fumarate to malate.
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Gordon Hammes
Gordon G. Hammes (born 1934 in Fond du Lac, Wisconsin) is a Distinguished Service Professor of Biochemistry, Emeritus, at Duke University, Professor Emeritus at Cornell University, and member of United States National Academy of Sciences.
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Kuo-Chen Chou
Kuo-Chen Chou (周国城) is a Chinese-born American Biophysics and Bioinformatics scientist.
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Manfred Eigen
Manfred Eigen (born 9 May 1927) is a German biophysical chemist who won the 1967 Nobel Prize in Chemistry for work on measuring fast chemical reactions.
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Mutation
In biology, a mutation is the permanent alteration of the nucleotide sequence of the genome of an organism, virus, or extrachromosomal DNA or other genetic elements.
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Natural selection
Natural selection is the differential survival and reproduction of individuals due to differences in phenotype.
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Product (chemistry)
Products are the species formed from chemical reactions.
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Protein engineering
Protein engineering is the process of developing useful or valuable proteins.
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Quantum tunnelling
Quantum tunnelling or tunneling (see spelling differences) is the quantum mechanical phenomenon where a particle tunnels through a barrier that it classically cannot surmount.
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Rate-determining step
In chemical kinetics, the overall rate of a reaction is often approximately determined by the slowest step, known as the rate-determining step (RDS) or rate-limiting step.
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Specificity constant
In the field of biochemistry, the specificity constant (also called kinetic efficiency or k_/K_), is a measure of how efficiently an enzyme converts substrates into products.
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Substrate (chemistry)
In chemistry, a substrate is typically the chemical species being observed in a chemical reaction, which reacts with a reagent to generate a product.
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Superoxide dismutase
Superoxide dismutase (SOD) is an enzyme that alternately catalyzes the dismutation (or partitioning) of the superoxide (O2&minus) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2).
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Triosephosphate isomerase
Triose-phosphate isomerase (TPI or TIM) is an enzyme that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate.
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References
[1] https://en.wikipedia.org/wiki/Diffusion_limited_enzyme