phosphoglycerate kinase

This role is performed by the enzyme phosphoglycerate kinase.

In most cases, phosphoglycerate kinase deficiency is inherited as an X-linked genetic trait.

Phosphoglycerate kinase 1 is an enzyme that in humans is encoded by the PGK1 gene.

During the reaction phosphoglycerate kinase undergoes a substrate induced conformational change similar to another metabolic enzyme called hexokinase.

Thus, ATP formation in Glycolysis is inhibited while bypassing the phosphoglycerate kinase reaction.

Nevertheless, in some proteins such as the yeast phosphoglycerate kinase and a mutant human ubiquitin, non-exponential kinetics suggesting downhill folding have been observed.

Angiostatin is produced, for example, by autoproteolytic cleavage of plasminogen, involving extracellular disulfide bond reduction by phosphoglycerate kinase.

The enzyme phosphoglycerate kinase catalyses the phosphorylation of 3-PGA by ATP (which was produced in the light-dependent stage).

Phylogenetic trees based on phosphoglycerate kinase (Pgk) amino acid sequences indicated a monophyletic origin for the Mollicutes within the Firmicutes.

Other deficiency diseases with similar signs and symptoms include deficiencies of phosphoglycerate kinase, phosphoglycerate mutase, lactate dehydrogenase, beta-enolase and aldolase A.

Phosphoglycerate kinase (PGK) deficiency is an X-linked recessive trait associated with hemolytic anemia, mental disorders and myopathy in humans.

The most familiar variant of glycolysis uses glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase to produce ATP.

As an insertion construct they used a fluorescing GFP gene driven by the ubiquitously expressed human phosphoglycerate kinase (PGK) promoter.

In complete reverse of the glycolytic pathway reaction, the enzyme phosphoglycerate kinase catalyses the reduction of the carboxyl group of 1,3BPG to form an aldehyde instead.

Glycolysis generates a net two molecules of ATP through substrate-level phosphorylation catalyzed by two enzymes: Phosphoglycerate kinase and pyruvate kinase.

During the payoff phase of glycolysis the enzymes phosphoglycerate kinase and pyruvate kinase facilitate the addition of a phosphate group to ADP by way of substrate level phosphorylation.

ATP is generated in a following separate step (key difference from oxidative phosphorylation) by transfer of the high-energy phosphate on 1,3-bisphosphoglycerate to ADP via the enzyme phosphoglycerate kinase, generating 3-phosphoglycerate.

M2-PK is a cytosolic enzyme that is associated with other glycolytic enzymes, i.e., hexokinase, glyceraldehyde 3-P dehydrogenase, phosphoglycerate kinase, phosphoglyceromutase, enolase, and lactate dehydrogenase within a so-called glycolytic enzyme complex.

A variety of enzymes are able to catalyze the final phosphorylation step for NRTIs, including nucleoside diphosphate kinase (NDP kinase), phosphoglycerate kinase, pyruvate kinase and creatine kinase, resulting in formation of respective antivirally active triphosphate analogues.

Anemia, Hemolytic with PGK Deficiency Erythrocyte Phosphoglycerate Kinase Deficiency PGK Phosphoglycerokinase None Phosphoglycerate kinase deficiency is an extremely rare inherited metabolic disorder characterized by deficiency of the enzyme phosphoglycerate kinase.