3zpx
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zpx OCA], [https://pdbe.org/3zpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zpx RCSB], [https://www.ebi.ac.uk/pdbsum/3zpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zpx ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zpx OCA], [https://pdbe.org/3zpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zpx RCSB], [https://www.ebi.ac.uk/pdbsum/3zpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zpx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The Ustilago maydis lipase UM03410 belongs to the mostly unexplored Candida antarctica lipase (CAL-A) subfamily. The two lipases with [corrected] the highest identity are a lipase from Sporisorium reilianum and the prototypic CAL-A. In contrast to the other CAL-A-type lipases, this hypothetical U. maydis lipase is annotated to possess a prolonged N-terminus of unknown function. Here, we show for the first time the recombinant expression of two versions of lipase UM03410: the full-length form (lipUMf) and an Nterminally truncated form (lipUMs). For comparison to the prototype, the expression of recombinant CAL-A in E. coli was investigated. Although both forms of lipase UM03410 could be expressed functionally in E. coli, the N-terminally truncated form (lipUMs) demonstrated significantly higher activities towards p-nitrophenyl esters. The functional expression of the N-terminally truncated lipase was further optimized by the appropriate choice of the E. coli strain, lowering the cultivation temperature to 20 degrees C and enrichment of the cultivation medium with glucose. Primary characteristics of the recombinant lipase are its pH optimum in the range of 6.5-7.0 and its temperature optimum at 55 degrees C. As is typical for lipases, lipUM03410 shows preference for long chain fatty acid esters with myristic acid ester (C14:0 ester) being the most preferred one.More importantly, lipUMs exhibits an inherent preference for C18:1Delta9 trans and C18:1Delta11 trans-fatty acid esters similar to CAL-A. Therefore, the short form of this U. maydis lipase is the only other currently known lipase with a distinct trans-fatty acid selectivity. | ||
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| + | The short form of the recombinant CAL-A-type lipase UM03410 from the smut fungus Ustilago maydis exhibits an inherent trans-fatty acid selectivity.,Brundiek H, Sass S, Evitt A, Kourist R, Bornscheuer UT Appl Microbiol Biotechnol. 2012 Apr;94(1):141-50. doi: 10.1007/s00253-012-3903-9., Epub 2012 Feb 1. PMID:022294433<ref>PMID:022294433</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3zpx" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Lipase 3D Structures|Lipase 3D Structures]] | *[[Lipase 3D Structures|Lipase 3D Structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
USTILAGO MAYDIS LIPASE UM03410, SHORT FORM WITHOUT FLAP
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