Enzyme Activity Measurement for 4-Hydroxybutyrate Dehydrogenase Using Spectrophotometric Assays

Creative Enzymes provides our customers with the first-rate service of enzyme activity measurement for 4-hydroxybutyrate dehydrogenase. The quality of our results is assured with the most advanced spectrophotometric instruments and a superb team with many brilliant scientists who have been working on enzyme activity assays for years.

4-Hydroxybutyrate dehydrogenase (EC1.1.1.61) is an enzyme that catalyzes the reversible reduction of 4-hydroxybutanoate to succinate semialdehyde, using NAD⁺ as the redox cofactor. The enzyme exists not only in bacteria but also in eukaryote, such as Arabidopsis thaliana, Escherichia coli, and Clostridium kluyveri. 4-Hydroxybutyrate dehydrogenase is a member from a group of oxidoreductases, which catalyze the CH-OH group of the substrate and use NAD⁺ or NADP⁺ as the cofactor. The systematic name of this enzyme class is 4-hydroxybutanoate: NAD⁺ oxidoreductase, which is also known as gamma-hydroxybutyrate dehydrogenase.

4-Hydroxybutyrate dehydrogenase plays a critical role in 4-aminobutanoate degradation V pathway. The 4-aminobutanoate degradation V pathway begins with the compound 4-aminobutanoate. 4-Aminobutanoate (GABA) is the major inhibitory neurotransmitter in the mammalian brain, and it has a role as a signaling molecule in plants as well. 4-Hydroxybutyrate dehydrogenase is the second enzyme of this pathway, which is a critical part of the superpathway of butanoate metabolism. Furthremore, 4-hydroxybutyrate dehydrogenase also poses a valuable function in some other important pathways, includingdegradation of the neurotransmitter 4-hydroxybutanoic acid, CO2 fixation in the Crenarchaeota pathway, and other metabolic pathways. Because of multiplecomplicated functions of this enzyme in various organisms, little conclusion has been achieved in understanding the activity and structure of the enzyme. While Creative Enzymes made the accurate activity assay available for 4-hydroxybutyrate dehydrogenase, based on years of experiences on testing the enzymes and optimizing the method. The spectrophotometric assay is considered to be the most reliable and cost-effective method for activity quantification. And the catalytic activity of 4-hydroxybutyrate dehydrogenase can be measured by following either the reduction of NAD⁺ at 260nm or the oxidation of NADH at 240nm, using spectrophotometric analysis.
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Figure: The crystal structure of 4-hydroxybutyrate dehydrogenase from Clostridium kluyveri. UniProt ID: P38945