3h6o
From Proteopedia
(Difference between revisions)
Line 8: | Line 8: | ||
<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=3h6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h6o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h6o RCSB], [http://www.ebi.ac.uk/pdbsum/3h6o 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=3h6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3h6o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3h6o RCSB], [http://www.ebi.ac.uk/pdbsum/3h6o 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]] | ||
Line 21: | Line 23: | ||
==See Also== | ==See Also== | ||
*[[Pyruvate Kinase|Pyruvate Kinase]] | *[[Pyruvate Kinase|Pyruvate Kinase]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 15:32, 25 December 2014
Activator-Bound Structure of Human Pyruvate Kinase M2
|
Categories: Homo sapiens | Pyruvate kinase | Arrowsmith, C H | Auld, D | Bochkarev, A | Bountra, C | Boxer, M | Dimov, S | Edwards, A M | Hong, B | Inglese, J | Jianq, J K | Min, S | Park, H | Structural genomic | Skoumbourdis, A | Southall, N | Tempel, W | Thomas, C | Weigelt, J | Activator | Allosteric enzyme | Glycolysis | Kinase | Magnesium | Metal-binding | Phosphoprotein | Pyruvate | Sgc | Transferase