4zv7: Difference between revisions
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tca|1tca]], [[1tcb|1tcb]], [[1tcc|1tcc]], [[3w9b|3w9b]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1tca|1tca]], [[1tcb|1tcb]], [[1tcc|1tcc]], [[3w9b|3w9b]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </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=4zv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zv7 OCA], [http://pdbe.org/4zv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zv7 RCSB], [http://www.ebi.ac.uk/pdbsum/4zv7 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=4zv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zv7 OCA], [http://pdbe.org/4zv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zv7 RCSB], [http://www.ebi.ac.uk/pdbsum/4zv7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zv7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4zv7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4zv7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Lipase|Lipase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:22, 6 October 2017
Crystal structure of hexagonal form of lipase B from Candida antarcticaCrystal structure of hexagonal form of lipase B from Candida antarctica
Structural highlights
Function[LIPB_CANAR] Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis. Publication Abstract from PubMedDuring crystallization screenings of commercially available hydrolytic enzymes, the new, hexagonal crystal form of CAL-B, has been discovered and hereby reported. The NAG molecules, which were closing the glycosylation site in the orthorhombic form, in hexagonal structure make the glycosylation site open. It is unknown whether the opening and closing of the glycosylation site by the 'lid' NAG molecules, could be related to the opening and closing of the active center of the enzyme upon substrate binding and product release. Crystal and molecular structure of hexagonal form of lipase B from Candida antarctica.,Strzelczyk P, Bujacz GD, Kielbasinski P, Blaszczyk J Acta Biochim Pol. 2015 Dec 30. PMID:26716135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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