Target type: molecularfunction
Catalysis of the reaction: 3-phospho-D-glycerate + ATP = 3-phospho-D-glyceroyl phosphate + ADP + H+. [EC:2.7.2.3, RHEA:14801]
Phosphoglycerate kinase (PGK) catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP, generating ATP and 3-phosphoglycerate. This reaction is a crucial step in glycolysis, the central metabolic pathway for energy production in most organisms. PGK plays a vital role in maintaining cellular energy homeostasis by coupling the energy released from the breakdown of glucose to the synthesis of ATP, the primary energy currency of cells.
The enzyme utilizes a two-step mechanism involving a phosphorylated intermediate. Initially, 1,3-BPG binds to PGK, and its phosphate group is transferred to a conserved histidine residue within the active site, forming a phosphohistidine intermediate. Subsequently, ADP binds to the enzyme, and the phosphate group is transferred from the phosphohistidine to ADP, generating ATP and releasing 3-phosphoglycerate.
PGK is a highly conserved enzyme across different species, and its structure and mechanism have been extensively studied. It is typically composed of two domains: an N-terminal domain that binds ADP and a C-terminal domain that binds 1,3-BPG. The active site is located at the interface of these domains, where the phosphohistidine intermediate is formed.
The activity of PGK is regulated by various factors, including substrate concentration, pH, and the presence of allosteric effectors. It is also subject to post-translational modifications, such as phosphorylation, which can modulate its activity.
In summary, phosphoglycerate kinase activity plays a vital role in energy metabolism by catalyzing the reversible transfer of a phosphate group from 1,3-BPG to ADP, generating ATP and 3-phosphoglycerate. This reaction is essential for maintaining cellular energy homeostasis and ensuring efficient energy production from glucose.'
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Protein | Definition | Taxonomy |
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Phosphoglycerate kinase 2 | A phosphoglycerate kinase 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P07205] | Homo sapiens (human) |
Phosphoglycerate kinase 1 | A phosphoglycerate kinase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P00558] | Homo sapiens (human) |
Phosphoglycerate kinase 2 | A phosphoglycerate kinase 2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P07205] | Homo sapiens (human) |
Phosphoglycerate kinase 1 | A phosphoglycerate kinase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P00558] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
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adenosine | quinquefolan B: isolated from roots of Panax quinquefolium L.; RN not in Chemline 10/87; RN from Toxlit | adenosines; purines D-ribonucleoside | analgesic; anti-arrhythmia drug; fundamental metabolite; human metabolite; vasodilator agent |
2-aminoadenosine | purine nucleoside | ||
n(6)-benzyladenosine | N(6)-benzyladenosine: RN given refers to parent cpd | ||
n(6)-cyclopentyladenosine |