Acetyl CoA Synthase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Acetyl CoA synthase catalyzes the conversion of acetate. ATP and coenzyme A into acetyl CoA and
AMP. This assay involves the chemical reaction between acetyl CoA and hydroxylamine which
liberates CoASH and hydroxamic acid which can be measured colorimetrically.
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Alanine Dehydrogenase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Alanine dehydrogenase catalyzes the oxidative deaminiation of L-alanine to pyruvate using NAD as
a co-substrate. This protocol describes a direct enzyme assay for determining alanine
dehydrogenase activity.
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Alcohol Dehydrogenase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Alcohol dehydrogenase catalyzes the oxidation of ethanol to acetaldehyde using NAD as a cosubstrate.
This protocol describes a direct enzyme assay for determining alcohol dehydrogenase
activity.
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Aminolevulinic Acid Synthase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Aminolevulinic acid synthase catalyzes the pyridoxal phosphate-dependent condensation of
succinyl coenzyme A and glycine to δ-Aminolevulinic acid. This protocol describes a coupled
enzyme assay for determining δ-aminolevulinic acid synthase activity.
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Citrate Synthase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Citrate synthase catalyzes the condensation of acetyl CoA and oxaloacetate to citrate and CoA. This
protocol describes an assay which uses DTNB. a chemical which reacts with sulfhydryl groups such
as that in the CoA generated in this enzymatic reaction.
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β-Galactosidase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: β-galactosidase catalyzes the hydrolysis of β-D-galactosides. such as the conversion of lactose to
galactose and glucose. Galactosides modified with compounds that are chromogenic can be used to
quantify the activity of β-galactosidase.
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Glucokinase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: This protocol describes an indirect assay to determine the activity of glucokinase. Glucose 6-phosphate formed by glucokinase is measured by the formation of NADPH in presence of glucose 6-phosphate dehydrogenase.
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Isocitrate Lyase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Isocitrate lyase catalyzes the hydrolysis of isocitrate into glyoxylate and succinate. This protocol
describes an assay which relies on a specific reaction of the product glyoxylate.
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Lactate Dehydrogenase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Lactate dehydrogenase catalyzes the reversible reduction of pyruvate to lactate using NADH as a cosubstrate.
This protocol describes a direct enzyme assay for determining lactate dehydrogenase
activity.
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Malate Dehydrogenase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Malate dehydrogenase catalyzes the reversible reduction of oxaloacetate to malate using NADH as a
co-substrate. This protocol describes a direct enzyme assay for determining malate dehydrogenase
activity.
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Malic Enzyme
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Malic enzyme (Malate dehydrogenase decarboxylating) catalyzes the oxidative carboxylation of Lmalate
to pyruvate using NAD as a co-substrate. This protocol describes a direct enzyme assay for
determining malic enzyme activity.
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NADH oxidase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: NADH oxidase catalyzes the oxidation of NADH to NAD with water as a co-product. This protocol
describes a direct enzyme assay measuring the quantity of NADH consumed. The co-substrate is
oxygen. and therefore the assay mixture must contain dissolved oxygen.
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PEP Carboxykinase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: PEP carboxykinase catalyzes the carboxylation of PEP to oxaloacetate with the generation of ATP.
In this coupled assay. the ATP generated by this reaction acts as a substrate in the conversion of 3-
phosphoglycerate to 1.3-diphosphoglycerate via the enzyme 3-phosphoglycerate phosphokinase.
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Phosphoenolpyruvate Carboxylase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Phosphoenolpyruvate carboxylase catalyzes the carboxylation of phosphoenolpyruvate to
oxaloacetate using carbonate as a co-substrate. This protocol describes a coupled enzyme assay for
determining phosphoenolpyruvate carboxylase activity.
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Pyruvate Carboxylase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Pyruvate carboxylase catalyzes the carboxylation of pyruvate to oxaloacetate using ATP and
carbonate as co-substrates. This protocol describes a coupled enzyme assay for determining
pyruvate carboxylase activity.
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Pyruvate Decarboxylase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Pyruvate decarboxylase catalyzes the oxidation of decarboxylation of pyruvate to acetaldehyde. This assay is an indirect method in which the conversion is linked to the activity of the subsequent enzyme alcohol dehydrogenase. which supplied in excess. converts the product acetaldehyde effectively into NAD and ethanol.
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Pyruvate Dehydrogenase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Pyruvate dehydrogenase is a component of the enzyme complex which catalyzes the conversion of
pyruvate to acetyl CoA and CO2 using NAD+ as the co-substrate. This protocol describes a coupled
assay to measure the pyruvate dehydrogenase activity.
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Pyruvate Kinase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: This protocol describes an indirect assay to determine the activity of pyruvate kinase. Pyruvate
formed from PEP by pyruvate kinase is measured by the formation of NAD+ in presence of
lactate dehydrogenase.
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Pyruvate Oxidase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Pyruvate oxidase catalyzes the oxidation of pyruvate to acetate and carbon dioxide. This protocol
describes the measurement of pyruvate oxidase based on the loss of absorbance of ferricyanide as it
oxidizes enzyme-bound flavin.
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Tyrosine Phenol Lyase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Tyrosine phenol lyase catalyzes the reversible conversion of tyrosine to phenol. pyruvate and
ammonium. This protocol describes a coupled enzyme assay involving an excess of lactate
dehydrogenase and NADH into the reaction mixture.
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Xylitol Dehydrogenase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Xylitol dehydrogenase catalyzes the oxidation of xylitol to xylulose using NAD+ as a co-substrate.
This protocol describes a direct enzyme assay for determining xylitol dehydrogenase activity.
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Xylose Reductase
Author:
Source: The University of Georgia. Department of Biological and Agricultural Engineering
Abstract: Xylitol reductase catalyzes the reduction D-xylose to xylitol using NADPH as a co-substrate. This
protocol describes a direct enzyme assay for determining xylitol reductase activity.
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