PGD
PGD (phosphogluconate dehydrogenase) is a cytoplasmic oxidoreductase that catalyses the oxidative decarboxylation of 6-phosphogluconate, producing ribulose 5-phosphate, CO2 and NADPH. It is the second dehydrogenase in the pentose phosphate shunt. Browse Assay Genie's current range of PGD research reagents below, or read on for the biology behind the target.
PGD catalyses the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, with concomitant reduction of NADP to NADPH. This reaction makes the enzyme the second dehydrogenase in the pentose phosphate shunt, a pathway that links glucose metabolism to the supply of reducing power in the form of NADPH.
The enzyme, formally named 6-phosphogluconate dehydrogenase, decarboxylating, is classified as EC 1.1.1.44 and sits within the HGNC gene group of oxidoreductases. UniProt places it in the 6-phosphogluconate dehydrogenase family, and it is found in the cytoplasm. The human PGD gene has mouse and rat orthologs, both named Pgd, which allows comparative work across common model species. NCBI Gene reports that several transcript variants encoding different isoforms have been described for this gene.
PGD has clinical relevance through inherited deficiency. According to the NCBI Gene summary, deficiency of this enzyme is generally asymptomatic and is inherited in an autosomal dominant manner. Haemolysis results from combined deficiency of 6-phosphogluconate dehydrogenase and 6-phosphogluconolactonase, which suggests a synergism between the two enzymopathies. Researchers studying NADPH production, pentose phosphate shunt flux or red cell enzymopathies therefore work with PGD as a defined enzymatic step.
PGD is the second dehydrogenase in the pentose phosphate shunt, making it a key enzyme for studying this branch of glucose metabolism.
The enzyme reduces NADP to NADPH while converting 6-phosphogluconate to ribulose 5-phosphate and CO2, linking it to cellular reducing power.
Combined deficiency of PGD and 6-phosphogluconolactonase causes haemolysis, pointing to a synergism between the two enzymopathies.
PGD deficiency is generally asymptomatic and autosomal dominant, providing a model for studying inherited defects in carbohydrate metabolism.
PGD catalyses the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO2, reducing NADP to NADPH. It is the second dehydrogenase in the pentose phosphate shunt and is located in the cytoplasm.
The HGNC name is phosphogluconate dehydrogenase, and UniProt lists 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44). No alternative symbols are recorded. NCBI Gene notes that several transcript variants encoding different isoforms have been found for this gene.
PGD deficiency is generally asymptomatic and autosomal dominant. Combined deficiency with 6-phosphogluconolactonase results in haemolysis. Mouse and rat both have a Pgd ortholog; check the datasheet of any product for its validated reactivity.
Other pentose phosphate pathway enzymes, NADPH-generating oxidoreductases and related metabolic targets with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P52209; product specifications from Assay Genie datasheets.