Creative Enzymes is the leading service institution in the enzyme activity measurement field. We provide reliable tests that exceed the average quality in the industry. The professional processes and high-quality services of Creative Enzymes support researchers and innovators in various activity assays for oxidoreductases, including glycerate dehydrogenase.

Glycerate dehydrogenase catalyzes the NADH-coupled reduction of hydroxypyruvate to D-glycerate, producing NAD+ as the byproduct. Alternatively, NADP+ can take the place of NAD+ in this reaction. In nature, this enzyme could also easily catalyze the reverse reaction as well. Glycerate dehydrogenase is also known as:

• D-glycerate dehydrogenase
• hydroxypyruvate reductase
• (R)-glycerate:NAD+ oxidoreductase

Glycerate dehydrogenase is a member of the enzyme family of NAD-dependent dehydrogenases that is characterized by a specificity for the D-isomer of the hydroxyacid substrate. This enzyme has a diverse range of original organisms and has been purified from bacterial, plant and mammalian sources. The structure of GDHs in plant and bacterial are shown to be the members of homologous family of 2-hydroxyacid dehydrogenases.

Figure: The crystal structure of a NAD-dependent D-glycerate dehydrogenase from Hyphomicrobium methylovorum.
Reference: Goldberg JD et al. J Mol Biol. 1994 4;236(4):1123-40

Glycerate dehydrogenase participates in glycine, serine and threonine metabolism, which are all important pathways in both human and micrioorganisms. And it is also involved in glyoxylate and dicarboxylate metabolism. The glyoxylate cycle shows an important subset of these reactions involved in biosynthesis of carbohydrates from fatty acids or two-carbon precursors, which enter the system as acetyl-coenzyme A. Therefore, as an important and key role in these pathways, glycerate dehydrogenase may show a prosperous prospect in synthetic biology. The studies on glycerate dehydrogenase may contribute to production of unnatural chemicals in microorganisms. Creative Enzymes offers professional enzyme activity assay of GHD to support such research and development activities. We use reliable spectrophotometric method to determine the enzyme activity of glycerate dehydrogenase, through detection of the consumption of NAD+ at 260 nm.

Creative Enzymes conducts and provides efficient and fast enzyme activity measurement. Our research center stands out with advanced equipment, rich experiences and a professional team, which assure high reproducibility and accuracy for the activity measurement. In the future, Creative Enzymes will continue to be your trust-worthy partner.