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DC Field | Value | Language |
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dc.citation.endPage | 1087 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 1081 | - |
dc.citation.title | NATURE CHEMICAL BIOLOGY | - |
dc.citation.volume | 13 | - |
dc.contributor.author | Oslund, Rob C | - |
dc.contributor.author | Su, Xiaoyang | - |
dc.contributor.author | Haugbro, Michael | - |
dc.contributor.author | Kee, Jung-Min | - |
dc.contributor.author | Esposito, Mark | - |
dc.contributor.author | David, Yael | - |
dc.contributor.author | Wang, Boyuan | - |
dc.contributor.author | Ge, Eva | - |
dc.contributor.author | Perlman, David H | - |
dc.contributor.author | Kang, Yibin | - |
dc.contributor.author | Muir, Tom W | - |
dc.contributor.author | Rabinowitz, Joshua D | - |
dc.date.accessioned | 2023-12-21T21:42:30Z | - |
dc.date.available | 2023-12-21T21:42:30Z | - |
dc.date.created | 2017-08-17 | - |
dc.date.issued | 2017-10 | - |
dc.description.abstract | Lower 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. | - |
dc.identifier.bibliographicCitation | NATURE CHEMICAL BIOLOGY, v.13, no.10, pp.1081 - 1087 | - |
dc.identifier.doi | 10.1038/nchembio.2453 | - |
dc.identifier.issn | 1552-4450 | - |
dc.identifier.scopusid | 2-s2.0-85031105485 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/22472 | - |
dc.identifier.url | https://www.nature.com/nchembio/journal/vaop/ncurrent/full/nchembio.2453.html | - |
dc.identifier.wosid | 000411135500012 | - |
dc.language | 영어 | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate | - |
dc.type | Article | - |
dc.description.isOpenAccess | FALSE | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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