4zv3: Difference between revisions
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''' | ==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4zv3]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZV3 FirstGlance]. <br> | |||
</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='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> | |||
[[Category: | </table> | ||
[[Category: Swarbrick, C | == Function == | ||
[[Category: | [[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> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Palmitoyl-CoA hydrolase]] | |||
[[Category: Forwood, J K]] | |||
[[Category: Swarbrick, C M.D]] | |||
[[Category: Double hotdog]] | |||
[[Category: Hydrolase]] | |||
[[Category: Inflammation]] | |||
[[Category: Thioesterase]] | |||
Revision as of 15:50, 3 June 2015
Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7Crystal structure of the N- and C-terminal domains of mouse acyl-CoA thioesterase 7
Structural highlights
Function[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.[1] References
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