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PGM is an isomerase enzyme, effectively transferring a phosphate group (PO 4 3−) from the C-3 carbon of 3-phosphoglycerate to the C-2 carbon forming 2-phosphoglycerate.There are a total of three reactions dPGM can catalyze: a mutase reaction resulting in the conversion of 3PG to 2PG and vice versa, [4] [5] a phosphatase reaction creating phosphoglycerate from 2,3-bisphosphoglycerate, [6] [7 ...
Phosphoglycolate phosphatase(EC 3.1.3.18; systematic name 2-phosphoglycolate phosphohydrolase), also commonly referred to as phosphoglycolate hydrolase, 2-phosphoglycolate phosphatase, P-glycolate phosphatase, and phosphoglycollate phosphatase, is an enzyme responsible for catalyzing the conversion of 2-phosphoglycolate into glycolate and phosphate:
Thus, the two substrates of this enzyme are 3-phospho-D-glyceroyl phosphate and (phosphate)n, whereas its two products are 3-phosphoglycerate and (phosphate)n+1. This enzyme belongs to the family of transferases , specifically those transferring phosphorus-containing groups ( phosphotransferases ) with a phosphate group as acceptor.
The enzyme phosphoglycerate phosphatase (EC 3.1.3.20) catalyzes the reaction D-glycerate 2-phosphate + H 2 O D-glycerate + phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is D-glycerate-2-phosphate phosphohydrolase.
Phosphoglycerate kinase (EC 2.7.2.3) (PGK 1) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP : 1,3-bisphosphoglycerate + ADP ⇌ glycerate 3-phosphate + ATP. Like all kinases it is a transferase.
Examples of mutases include bisphosphoglycerate mutase, which appears in red blood cells and phosphoglycerate mutase, which is an enzyme integral to glycolysis. In glycolysis, it changes 3-phosphoglycerate to 2-phosphoglycerate by moving a single phosphate group within a single molecule.
3-phosphoglycerate dehydrogenase works via an induced fit mechanism to catalyze the transfer of a hydride from the substrate to NAD+, a required cofactor.In its active conformation, the enzyme's active site has multiple cationic residues that likely stabilize the transition state of the reaction between the negatively charged substrate and NAD +.
In enzymology, a phosphoglycerate kinase (GTP) (EC 2.7.2.10) is an enzyme that catalyzes the chemical reaction. GTP + 3-phospho-D-glycerate GDP + 3-phospho-D-glyceroyl phosphate. Thus, the two substrates of this enzyme are GTP and 3-phospho-D-glycerate, whereas its two products are GDP and 3-phospho-D-glyceroyl phosphate.