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Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate.

Author(s): Oslund, Rob C; Su, Xiaoyang; Haugbro, Michael; Kee, Jung-Min; Esposito, Mark; et al

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dc.contributor.authorOslund, Rob Cen_US
dc.contributor.authorSu, Xiaoyangen_US
dc.contributor.authorHaugbro, Michaelen_US
dc.contributor.authorKee, Jung-Minen_US
dc.contributor.authorEsposito, Marken_US
dc.contributor.authorDavid, Yaelen_US
dc.contributor.authorWang, Boyuanen_US
dc.contributor.authorGe, Evaen_US
dc.contributor.authorPerlman, David Hen_US
dc.contributor.authorKang, Yibinen_US
dc.contributor.authorMuir, Tom Wen_US
dc.contributor.authorRabinowitz, Joshua Den_US
dc.date.accessioned2020-02-29T03:39:09Z-
dc.date.available2020-02-29T03:39:09Z-
dc.date.issued2017-10en_US
dc.identifier.citationOslund, Rob C, Su, Xiaoyang, Haugbro, Michael, Kee, Jung-Min, Esposito, Mark, David, Yael, Wang, Boyuan, Ge, Eva, Perlman, David H, Kang, Yibin, Muir, Tom W, Rabinowitz, Joshua D. (2017). Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate.. Nature chemical biology, 13 (10), 1081 - 1087. doi:10.1038/nchembio.2453en_US
dc.identifier.issn1552-4450en_US
dc.identifier.urihttp://arks.princeton.edu/ark:/88435/pr15z02-
dc.description.abstractLower glycolysis involves a series of reversible reactions, which interconvert intermediates that also feed anabolic pathways. 3-phosphoglycerate (3-PG) is an abundant lower glycolytic intermediate that feeds serine biosynthesis via the enzyme phosphoglycerate dehydrogenase, which is genomically amplified in several cancers. Phosphoglycerate mutase 1 (PGAM1) catalyzes the isomerization of 3-PG into the downstream glycolytic intermediate 2-phosphoglycerate (2-PG). PGAM1 needs to be histidine phosphorylated to become catalytically active. We show that the primary PGAM1 histidine phosphate donor is 2,3-bisphosphoglycerate (2,3-BPG), which is made from the glycolytic intermediate 1,3-bisphosphoglycerate (1,3-BPG) by bisphosphoglycerate mutase (BPGM). When BPGM is knocked out, 1,3-BPG can directly phosphorylate PGAM1. In this case, PGAM1 phosphorylation and activity are decreased, but nevertheless sufficient to maintain normal glycolytic flux and cellular growth rate. 3-PG, however, accumulates, leading to increased serine synthesis. Thus, one biological function of BPGM is controlling glycolytic intermediate levels and thereby serine biosynthetic flux.en_US
dc.format.extent1081 - 1087en_US
dc.languageengen_US
dc.relation.ispartofNature chemical biologyen_US
dc.titleBisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate.en_US
dc.typeJournal Article-
dc.identifier.doidoi:10.1038/nchembio.2453en_US
dc.identifier.eissn1552-4469en_US
pu.type.symplectichttp://www.symplectic.co.uk/publications/atom-terms/1.0/journal-articleen_US

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