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Enzyme Activity Measurement for Phosphoglycerate Kinase

Creative Enzymes is a leading service provider specialized in measuring enzyme activities. Having tested numerous enzyme activities in the past several years, Creative Enzymes has accumulated extensive experience, which can provide rapid and high-quality enzyme activity assay services for all types of transferases, such as phosphoglycerate kinase.

Phosphoglycerate kinase (EC 2.7.2.3; PGK) is an enzyme that catalyzes the ATP-dependent phosphorylation of 3-phospho-glycerate (3-PG) to 1,3-bisphosphoglycerate (1,3-bisPG), in a reversible reaction requiring Mg2+ as an essential cofactor. The enzyme is found in all organisms, with the presence of forms localizing in different intracellular compartments. In photosynthetic organisms, the PGK enzyme plays a pivotal role in catalyzing the step following carbon fixation by the Calvin-Benson cycle. PGK also serves as one of the two ATP-generating enzymes in glycolysis. In the gluconeogenic pathway, PGK catalyzes the reverse reaction, while the glycolytic direction is preferred under biochemical standard conditions.

The molecular structure of PGK is strongly conserved in all species studied so far. PGK is a monomeric enzyme having two domains, an N-terminal domain and C-terminal domain connected by a linker α-helix. Conformational changes controlling interactions between the two domains initiate the transfer of the phosphate group. In humans, PGK is divided into two isoforms, PGK1 and PGK2.

PGK deficiency has been reported to be associated with hemolytic anemia, mental disorders, and myopathy in humans. Moreover, PGK1 overexpression has been found to be related to gastric cancer. Furthermore, PGK also plays a critical role in the phosphorylation and activation of HIV antiretroviral drugs due to its wide specificity towards nucleotide substrates. Therefore, PGK is getting more and more attentions from pharmaceutical companies and biotechnology institutes. To investigate the functional significance of PGK smoothly, it is necessary to be able to accurately monitor the activity of PGK. Herein, Creative Enzymes provides the meticulous enzymatic assay for PGK. We measure PGK activity using the coupled reaction with glyceraldehyde-3-phosphate dehydrogenase from the previous step of the glycolytic pathway. NADH consumption is monitored as a function of time by following the absorbance at 340 nm. The services of Creative Enzymes are the most trusted and proven in the market, and have been commended by many customers. Creative Enzymes will always be your trusty-worthy partner and continue supporting your goal of industrialization and commercialization of the enzyme.

Figure: The  crystal structure of the E. coli  phosphoglycerate kinase. This structure  shows the presence of two globular domains, N-domain (silver) and C-domain  (gold) connected by a α-helix linker (brown) Figure: The crystal structure of the E. coli phosphoglycerate kinase. This structure shows the presence of two globular domains, N-domain (silver) and C-domain (gold) connected by a α-helix linker (brown).
Reference: Young T A, Skordalakes E, Marqusee S. Journal of molecular biology, 2007, 368(5): 1438-1447.



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