
Phosphoglycerate kinase - Wikipedia
PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, generating ADP and 1,3-BPG. In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2.
Phosphoglycerate kinase: structural aspects and functions, with …
Phosphoglycerate kinase (PGK) is a glycolytic enzyme that is well conserved among the three domains of life. PGK is usually a monomeric enzyme of about 45 kDa that catalyses one of the two ATP-producing reactions in the glycolytic pathway, through the conversion of 1,3-bisphosphoglycerate (1,3BPGA) to 3-phosphoglycerate (3PGA).
Phosphoglycerate kinase: structural aspects and functions ... - PubMed
In this review, we have highlighted the overall aspects of this enzyme, such as its structure, reaction kinetics, activity regulation and possible moonlighting functions in different protistan organisms, especially both free-living and parasitic Kinetoplastea.
PGK1 Gene - GeneCards | PGK1 Protein | PGK1 Antibody
Dec 25, 2024 · PGK1 (Phosphoglycerate Kinase 1) is a Protein Coding gene. Diseases associated with PGK1 include Phosphoglycerate Kinase 1 Deficiency and Nonaka Myopathy. Among its related pathways are glycolysis (BioCyc) and Gluconeogenesis. Gene Ontology (GO) annotations related to this gene include phosphoglycerate kinase activity.
The basic functions of phosphoglycerate kinase 1 and its roles in ...
Apr 5, 2022 · Phosphoglycerate kinase 1 (PGK1) is an essential enzyme that catalyzes adenosine 5′-triphosphate (ATP) production in aerobic glycolysis.
Structure, function, and folding of phosphoglycerate kinase are ...
Oct 4, 2010 · Phosphoglycerate kinase (PGK) is a 415-residue metabolic enzyme that produces ATP and is composed of two roughly equally sized subunits connected by a flexible hinge (1). In the crystal structure, the ADP and diphosphoglycerate binding sites, each located at an N and C subunit, are separated.
UniProt
Jan 23, 2007 · In addition to its role as a glycolytic enzyme, it seems that PGK1 acts as a polymerase alpha cofactor protein (primer recognition protein) (PubMed: 2324090).
Molecular mechanism of glycolytic flux control intrinsic to human ...
Here, we report a protein-level regulation of human PGK (hPGK) by utilizing the switching ligand-binding cooperativities between adenine nucleotides and 3-phosphoglycerate (3PG). This was revealed by nuclear magnetic resonance (NMR) spectroscopy at physiological salt concentrations.
Phosphoglycerate Kinase - an overview | ScienceDirect Topics
Phosphoglycerate kinase (PGK) is an ATP-generating step of the glycolytic pathway through reversible transfer of a phosphate group from 1,3-bisphosphoglycerate to ADP. Glycerate-3-phosphate is produced from 1,3-bisphophoglycerate and continues in glycolysis as the carbon backbone to eventually yield pyruvate.
(PDF) Phosphoglycerate kinase: structural aspects and functions, …
Nov 25, 2020 · Phosphoglycerate kinase (PGK) is a glycolytic enzyme that is well conserved among the three domains of life. PGK is usually a monomeric enzyme of about 45 kDa that catalyses one of the two...