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Richards_CH09x
Richards_CH09x

... – The drug isoniazid, for example, is used in the treatment of tuberculosis and is detoxified through the addition of an acetyl group onto the molecule (acetylation reaction) mediated via the enzyme N-acetyl-transferase. – Individuals that have the normal form of this enzyme can eliminate a dose by ...
06B Enzyme (Pressure)
06B Enzyme (Pressure)

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Inhibition of E. coli l-Asparaginase by Reaction with 2, 3
Inhibition of E. coli l-Asparaginase by Reaction with 2, 3

... ment we have no idea on the mechanism of the eli­ m ination of histidine residues by reaction of the en­ zyme with 2,3-butanedione. We would like to re­ member, however, that this is not the first example of absolutly unexpected loss of am ino acids observed in the course of modification experiments ...
Crystal Structure Sheds Light on Hereditary Coproporphyria
Crystal Structure Sheds Light on Hereditary Coproporphyria

... molecules like oxygen (globins), carbon monoxide (CO) (cytochrome oxidase), and nitric oxide (NO) (soluble guanylyl cyclase) (2,3). With the exception of a few microorganisms, heme is found in all three archaea, prokarya, and eukarya kingdoms (2). On the one hand, heme biosynthesis is a sine qua non ...
Properties of an Enzyme: Acid Phosphatase
Properties of an Enzyme: Acid Phosphatase

... Experiment #10 Objective To show the catalysis of a chemical reaction by an active enzyme and to observe the effects of temperature, killing the enzyme with heat, concentration of substrate, and the presence of an inhibitor of the enzyme. Introduction Phosphatases catalyze the hydrolysis of phosphat ...
Single-enzyme approach predicts natural emergence of
Single-enzyme approach predicts natural emergence of

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Essential Bioinformatics and Biocomputing (LSM2104: Section I
Essential Bioinformatics and Biocomputing (LSM2104: Section I

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Free Energy Surface of the Michaelis Complex of Lactate

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Diiffusional correlations among multiple active sites in a single enzyme
Diiffusional correlations among multiple active sites in a single enzyme

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Enzyme Article
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Stereochemistry: Atropisomers

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Influence of Environment Modifications on Enzyme Catalysis
Influence of Environment Modifications on Enzyme Catalysis

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Enzymes and Lactose Intolerance - Science Take-Out
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Pentose phosphate pathway (hexose monophosphate shunt)
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... decarboxylation to give a pentose, ribulose 5‐phosphate, which is  converted to its isomer, D‐ribose 5‐phosphate. ‐ Overall equation of 1st phase: Glucose 6‐phosphate + 2 NADP++ H2O ribose 5‐phosphate + CO2 + 2 NADPH + 2 H+ ...
ENZYME ACTION - Southern Biological
ENZYME ACTION - Southern Biological

... Organisms including humans use amylase to break down dietary starch to render it soluble and to allow it to be absorbed during digestion. Many industrial processes also use amylase. For example, it is sometimes used in brewing to remove haziness caused by residual (insoluble) starch in beer. Investi ...
beta-glucanase
beta-glucanase

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Enzyme Lab
Enzyme Lab

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for ESL students
for ESL students

... they would die. In fact, your cells are always making poisonous chemicals. They do not die because your cells use enzymes to break down these poisonous chemicals into harmless substances. Enzymes are proteins that speed up the rate of reactions that would otherwise happen more slowly. The enzyme is ...
potassium in tomato
potassium in tomato

... Role and Deficiency Symptoms of Potassium in Tomato Introduction Potassium is used in carbohydrate metabolism and increases water-use efficiency It is essential for protein synthesis and activates enzymes and controls their reaction rates It promotes flower and fruit production and is vital for ...
Molecular dynamics simulations of active site mutants of rat
Molecular dynamics simulations of active site mutants of rat

... during the MD. The substrate orients with the guanidinium group toward the metals with a distance of approximately 4.5 Å. The carbon chain of the arginine is approximately 4 Å from His141. The carboxyl group is about 3.6 Å from Asp 181 and 6.2 Å from Gly18. After optimization, the substrate was seen ...
1/(V/Km)
1/(V/Km)

... the velocity at steady-state is given by the equation v = k2[Et][S] / ((k-1 + k2)/k1 + [S]) = V[S] / (Km + [S]) where V = k2[Et] and is thus a function of total enzyme concentration, and Km = (k-1 + k2)/k1 is derived from multiple rate constants. The complexity of this term increases for more compli ...
Presentasi 1
Presentasi 1

... Ag binding site on Ab binds to Ag complementally, no further reaction occurs. ...
Chapter 5
Chapter 5

... Enzymes have a specific shape that fits with the substrate shape. ...
The effect of calcium on conformational change of thimet
The effect of calcium on conformational change of thimet

... closed shape, and therefore inactive. In this study, the inhibitors used were either the first or second half of a substrate. The reason that there is a difference between the two is because of how the different inhibitors bind in the active site, and more specifically which end of them is interacti ...
The Citric Acid Cycle
The Citric Acid Cycle

... energy change for hydrolyzing succinyl-CoA into succinate and coenzyme A is -33.8 kJ/mole. The standard free energy required to synthesize GTP from GDP and Pi is +30.5 kJ/mole. If we couple these two reactions together than the standard free energy change is -3.3 kJ/mole. This enzyme catalyzes a sub ...
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Isomerase



Isomerases are a general class of enzymes which convert a molecule from one isomer to another. Isomerases can either facilitate intramolecular rearrangements in which bonds are broken and formed or they can catalyze conformational changes. The general form of such a reaction is as follows:A–B → B–AThere is only one substrate yielding one product. This product has the same molecular formula as the substrate but differs in bond connectivity or spatial arrangements. Isomerases catalyze reactions across many biological processes, such as in glycolysis and carbohydrate metabolism.
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