3g2g
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3g2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3g2g RCSB], [http://www.ebi.ac.uk/pdbsum/3g2g PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3g2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g2g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3g2g RCSB], [http://www.ebi.ac.uk/pdbsum/3g2g PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/KPYM_HUMAN KPYM_HUMAN]] Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio betwween the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival.<ref>PMID:17308100</ref> <ref>PMID:18191611</ref> <ref>PMID:21620138</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Pyruvate Kinase|Pyruvate Kinase]] | *[[Pyruvate Kinase|Pyruvate Kinase]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 06:44, 25 December 2014
S437Y Mutant of human muscle pyruvate kinase, isoform M2
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Categories: Homo sapiens | Pyruvate kinase | Allali-Hassani, A | Arrowsmith, C H | Bochkarev, A | Bountra, c | Dimov, S | Edwards, A M | Hong, B | MacKenzie, F | Park, H | Structural genomic | Tempel, W | Vedadi, M | Weigelt, J | Allosteric enzyme | Glycolysis | Kinase | Magnesium | Metal-binding | Mutation | Phosphoprotein | Pyruvate | Single nucleotide polymorphism | Snp | Transferase