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4zv3
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==Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7== | ==Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7== | ||
<StructureSection load='4zv3' size='340' side='right' caption='[[4zv3]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='4zv3' size='340' side='right' caption='[[4zv3]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Palmitoyl-CoA_hydrolase Palmitoyl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.2 3.1.2.2] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Palmitoyl-CoA_hydrolase Palmitoyl-CoA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.2 3.1.2.2] </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=4zv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zv3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4zv3 RCSB], [http://www.ebi.ac.uk/pdbsum/4zv3 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=4zv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zv3 OCA], [http://pdbe.org/4zv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zv3 RCSB], [http://www.ebi.ac.uk/pdbsum/4zv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zv3 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BACH_MOUSE BACH_MOUSE]] Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.<ref>PMID:11834298</ref> | [[http://www.uniprot.org/uniprot/BACH_MOUSE BACH_MOUSE]] Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl-CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA.<ref>PMID:11834298</ref> | ||
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| + | ==See Also== | ||
| + | *[[Thioesterase|Thioesterase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:00, 10 March 2017
Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7
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