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Phosphoglycerate kinase mechanism in glycolysis. Without either substrate bound, PGK exists in an "open" conformation . After both the triose and nucleotide substrates are bound to the N- and C-terminal domains, respectively, an extensive hinge-bending motion occurs, bringing the domains and their bound substrates into close proximity and ...
5230 18655 Ensembl ENSG00000102144 ENSMUSG00000062070 UniProt P00558 P09411 RefSeq (mRNA) NM_000291 NM_008828 RefSeq (protein) NP_000282 NP_032854 Location (UCSC) Chr X: 77.91 – 78.13 Mb Chr X: 105.23 – 105.25 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Phosphoglycerate kinase 1 is an enzyme that in humans is encoded by the PGK1 gene. Interactive pathway map Click on genes ...
This step is the enzymatic transfer of a phosphate group from 1,3-bisphosphoglycerate to ADP by phosphoglycerate kinase, forming ATP and 3-phosphoglycerate. At this step, glycolysis has reached the break-even point: 2 molecules of ATP were consumed, and 2 new molecules have now been synthesized.
2 play other amplifying roles in glycolysis in hepatocytes. Other transacting factors suspected of playing a role in liver cell transcription regulation include: Hepatic nuclear factor-4-alpha is an orphan nuclear receptor important in the transcription of many genes for enzymes of carbohydrate and lipid metabolism.
Other names in common use include glucose-phosphate kinase, phosphoglucokinase (phosphorylating), and ATP:D-glucose-1-phosphate 6-phosphotransferase. This enzyme participates in starch and sucrose metabolism .
GAPN is used in a variant of glycolysis that conserves energy as NADPH rather than as ATP. The NADPH and 3-PG can then be used for synthesis. The most familiar variant of glycolysis uses glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase to produce ATP. GAPDH is phosphorylating. GAPN is non-phosphorylating.
Substrate-level phosphorylation exemplified with the conversion of ADP to ATP. Substrate-level phosphorylation is a metabolism reaction that results in the production of ATP or GTP supported by the energy released from another high-energy bond that leads to phosphorylation of ADP or GDP to ATP or GTP (note that the reaction catalyzed by creatine kinase is not considered as "substrate-level ...
2,3-BPG is formed from 1,3-BPG by the enzyme BPG mutase.It can then be broken down by 2,3-BPG phosphatase to form 3-phosphoglycerate.Its synthesis and breakdown are, therefore, a way around a step of glycolysis, with the net expense of one ATP per molecule of 2,3-BPG generated as the high-energy carboxylic acid-phosphate mixed anhydride bond is cleaved by 2,3-BPG phosphatase.