4p69
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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [http://www.ebi.ac.uk/pdbsum/4p69 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57]] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Jimin, Z | + | [[Category: Jimin, Z]] |
| - | [[Category: Nan, W | + | [[Category: Nan, W]] |
| - | [[Category: Shu, W | + | [[Category: Shu, W]] |
| - | [[Category: Zongchao, J | + | [[Category: Zongchao, J]] |
[[Category: Hydrolase-oxidoreductase complex]] | [[Category: Hydrolase-oxidoreductase complex]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 20:38, 25 December 2014
Acek (D477A) ICDH complex
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