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  Encyclopedia of Keywords > Biochemistry > Molecular Biology > Proteins > Enzymes > Enzyme   Michael Charnine

Keywords and Sections
ENZYMES
ENZYME KINETICS
ENZYME REACTION
SUBSTRATE
INHIBITORS
SATURATION CURVE
EQUATION
ENZYME ASSAYS
BIND
KINETIC PARAMETERS
CATALYTIC
PHOSPHATE
PYRUVATE CARBOXYLASE
NADH
ENZYME PRODUCES
ENZYME ACTIVITY
SATURATED
REACTION MECHANISMS
REACT
PRODUCT
ENZYME DATABASE
PLP
HYDROLYTIC ENZYME
ENZYME SUBSTRATE
ENZYME
Review of Short Phrases and Links

    This Review contains major "Enzyme"- related terms, short phrases and links grouped together in the form of Encyclopedia article.

Definitions

  1. An enzyme is a protein, or protein complex, that catalyzes a chemical reaction.
  2. The enzyme is a homodimer comprising of two 99 residue monomers with a substrate cleavage site located at the interface between them. (Web site)
  3. An enzyme is a protein that acts as a catalyst. (Web site)
  4. ENZYME is a repository of information related to the nomenclature of enzymes.
  5. Enzyme: A protein that speeds up chemical reactions in the body.

Enzymes

  1. Helicase is an enzyme vital to all living organisms. (Web site)
  2. Phosphofructokinase is the most important enzyme for control of glycolysis. (Web site)
  3. This enzyme converts a portion of the glucose into fructose thus making it sweeter.
  4. X-ray studies on penicillinase enzyme. (Web site)

Enzyme Kinetics

  1. The particular type of an inhibitor can be discerned by studying the enzyme kinetics as a function of the inhibitor concentration.
  2. Enzyme kinetics is the study of the rates of chemical reactions that are catalysed by enzymes.
  3. In 1913, Leonor Michaelis and Maud Menten proposed a quantitative theory of enzyme kinetics, which is referred to as Michaelis-Menten kinetics.

Enzyme Reaction

  1. Most enzyme kinetics studies concentrate on this initial, linear part of enzyme reactions.
  2. The Michaelis constant K m is defined as the concentration at which the rate of the enzyme reaction is half V max.
  3. Enzyme reactions involving more than one substrate 5.1 Michaelis-Menten kinetics 5.2 Michaelis-Menten kinetics of a two-substrate reaction 6. (Web site)

Substrate

  1. With increasing substrate concentration [S], the enzyme is asymptotically approaching its maximum speed V max, but never actually reaching it.
  2. As enzyme-catalysed reactions are saturable, their rate of catalysis does not show a linear response to increasing substrate.
  3. This is given by the Michaelis-Menten constant ( K m), which is the substrate concentration required for an enzyme to reach one-half its maximum velocity.

Inhibitors

  1. Reversible enzyme inhibitors can be classified as competitive, uncompetitive, non-competitive or mixed, according to their effects on K m and V max.
  2. Enzyme inhibitors can also irreversibly inactivate enzymes, usually by covalently modifying active site residues.
  3. Not all irreversible inhibitors form covalent adducts with their enzyme targets. (Web site)

Saturation Curve

  1. Michaelis---Menten kinetics Saturation curve for an enzyme showing the relation between the concentration of substrate and rate.
  2. Non-Michaelis---Menten kinetics Main article: Allosteric regulation Saturation curve for an enzyme reaction showing sigmoid kinetics. (Web site)

Equation

  1. This Michaelis-Menten equation is the basis for most single-substrate enzyme kinetics.
  2. Equations such as the Michaelis-Menten equation describe how this slope varies with the substrate and enzyme concentrations.
  3. Both the Lineweaver-Burk and Eadie-Hofstee transformation of the Michaelis-Menton equation are useful in the analysis of enzyme inhibition.

Enzyme Assays

  1. Enzyme assays are laboratory procedures that measure the rate of enzyme reactions.
  2. Enzyme assays are usually set up to produce an initial rate lasting over a minute, to make measurements easier.
  3. The most sensitive enzyme assays use lasers focused through a microscope to observe changes in single enzyme molecules as they catalyse their reactions.
  4. Enzyme assays are laboratory methods for measuring enzymatic activity. (Web site)

Bind

  1. In these enzymes, both substrates bind to the enzyme at the same time to produce an EAB ternary complex.
  2. These target molecules bind to an enzyme's active site and are transformed into products through a series of steps known as the enzymatic mechanism.
  3. Some reversible inhibitors bind so tightly to their target enzyme that they are essentially irreversible. (Web site)
  4. The binding with an allosteric activator activates an enzyme molecule because the active site is in the right conformation to bind with substrate molecules.

Kinetic Parameters

  1. An introduction to enzyme kinetics An accessible set of on-line tutorials on enzyme kinetics.
  2. If the enzyme obeys Michaelis-Menten kinetics the kinetic parameters k 0 and k A often behave similarly.
  3. Post a question or answer questions about "enzyme kinetics" at WikiAnswers. (Web site)

Catalytic

  1. ExCatDB A database of enzyme catalytic mechanisms.
  2. The amino acids sidechains which make up the active site are molded into a precise shape which enables the enzyme to perform its catalytic function.

Phosphate

  1. The fructose-6-phosphate can be converted by the enzyme, hexose phosphate isomerase into glucose-6-phosphate.
  2. E. N-acetyl glutamate is a positive effector of the enzyme catalyzing the synthesis of carbamoyl phosphate.

Pyruvate Carboxylase

  1. Recently biochemistry has focused more specifically on the chemistry of enzyme -mediated reactions, and on the properties of proteins.
  2. The reaction catalysed by an enzyme uses exactly the same reactants and produces exactly the same products as the uncatalysed reaction.
  3. Mechanisms of catalysis The energy variation as a function of reaction coordinate shows the stabilisation of the transition state by an enzyme. (Web site)
  4. The enzyme dihydrolipoyl dehydrogenase, with FAD + as a cofactor, catalyzes that oxidation reaction.
  5. This reaction is catalysed by pyruvate carboxylase, an enzyme activated by Acetyl-CoA, indicating a lack of oxaloacetate.

Nadh

  1. The electron is used to reduce the co-enzyme NADH, which has functions in the light-independent reaction.
  2. One NADH molecule is reduced by the enzyme glutamate dehydrogenase in the conversion of glutamate to ammonium and a-ketoglutarate.

Enzyme Produces

  1. The enzyme produces product at a linear initial rate at the start of the reaction.
  2. In the figure to the right, the enzyme produces E* rapidly in the first few seconds of the reaction.

Enzyme Activity

  1. Enzyme inhibitors are molecules that reduce or abolish enzyme activity.
  2. Includes competitive inhibition, enzyme cofactors, a closer look at factors affecting enzyme action, and regulation of enzyme activity.

Saturated

  1. This can continue until all the enzyme becomes saturated with substrate and the rate reaches a maximum.
  2. In this state, all enzyme active sites are saturated with substrate.

Reaction Mechanisms

  1. MACiE A database of enzyme reaction mechanisms.
  2. Superb animations of several enzyme reaction mechanisms.

React

  1. Only after the first substrate is released can substrate B bind and react with the modified enzyme, regenerating the unmodified E form.
  2. Thus, the specificity constant is an effective bimolecular rate constant for free enzyme to react with free substrate to form product.

Product

  1. The speed V means the number of reactions per second that are catalyzed by an enzyme.
  2. The enzymatic reaction is supposed to be irreversible, and the product does not rebind the enzyme.
  3. After the catalytic reaction, the product is then passed on to another enzyme.
  4. Recently, biochemistry has focused more specifically on the chemistry of enzyme - catalyzed reactions, and on the properties of proteins.
  5. The catalyzed reaction takes place in only a small part of the enzyme called the active site.

Enzyme Database

  1. BRENDA Comprehensive enzyme database, giving substrates, inhibitors and reaction diagrams.
  2. Related Links BRENDA, the enzyme database: updates and major new developments.

Plp

  1. PLP together with the enzyme phosphorylase is responsible for the breakdown of glycogen. (Web site)
  2. An enzyme is required to effect this transformation and the enzymes employs a co-factor (or prosthetic group).This cofactor is pyridoxal phosphate (PLP).

Hydrolytic Enzyme

  1. It is understood that the name of the substrate with this suffix means a hydrolytic enzyme.
  2. P. purpurogenum was found to produce both extracellular and intracellular fructosyltransferase and sucrose hydrolytic enzyme. (Web site)

Enzyme Substrate

  1. The enzyme itself is not used up in the process, and is free to catalyze the same reaction with a new set of substrates.
  2. In a metabolic pathway, one enzyme takes the product of another enzyme as a substrate.
  3. Enzyme intermediates contain substrates A and B or products P and Q.
  4. Negative cooperativity occurs when binding of the first substrate decreases the affinity of the enzyme for other substrate molecules.
  5. In such mechanisms, substrate A binds, changes the enzyme to E* by, for example, transferring a chemical group to the active site, and is then released.

Enzyme

  1. This is the maximum velocity ( V max) of the enzyme.
  2. Phenylalanine hydroxylase is the rate-limiting enzyme of the metabolic pathway which degrades excess phenylalanine.
  3. The methanogens fix CO 2 by means of the enzyme CODH ( carbon monoxide dehydrogenase) and the Acetyl CoA pathway (Figure 23 below).
  4. Enzyme turnover rates, Michaelis-Menten kinetics, receptor binding, Hill coefficient. (Web site)
  5. Ribbon diagram of the catalytically perfect enzyme TIM.

Categories

  1. Biochemistry > Molecular Biology > Proteins > Enzymes
  2. Encyclopedia of Keywords > Nature > Chemistry > Molecules
  3. Encyclopedia of Keywords > Nature > Chemistry
  4. Encyclopedia of Keywords > Nature > Life > Animals
  5. Society > Humans > Health > Diseases
  6. Books about "Enzyme" in Amazon.com

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  Short phrases about "Enzyme"
  Originally created: September 14, 2007.
  Links checked: February 28, 2013.
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