4ufq: Difference between revisions
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.35 3.2.1.35] </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=4ufq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ufq OCA], [http://pdbe.org/4ufq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ufq RCSB], [http://www.ebi.ac.uk/pdbsum/4ufq 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=4ufq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ufq OCA], [http://pdbe.org/4ufq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ufq RCSB], [http://www.ebi.ac.uk/pdbsum/4ufq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ufq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
Hyaluronidases (Hyals) are broadly used in medical applications to facilitate the dispersion and/or absorption of fluids or medications. This study reports the isolation, cloning, and industrial-scale recombinant production, purification and full characterization, including X-ray structure determination at 1.45 A, of an extracellular Hyal from the nonpathogenic bacterium Streptomyces koganeiensis. The recombinant S. koganeiensis Hyal (rHyal_Sk) has a novel bacterial catalytic domain with high enzymatic activity, compared with commercially available Hyals, and is more thermostable and presents higher proteolytic resistance, with activity over a broad pH range. Moreover, rHyal_Sk exhibits remarkable substrate specificity for hyaluronic acid (HA) and poses no risk of animal cross-infection. | |||
Identification and characterization of a bacterial hyaluronidase and its production in recombinant form.,Messina L, Gavira JA, Pernagallo S, Unciti-Broceta JD, Sanchez Martin RM, Diaz-Mochon JJ, Vaccaro S, Conejero-Muriel M, Pineda-Molina E, Caruso S, Musumeci L, Di Pasquale R, Pontillo A, Sincinelli F, Pavan M, Secchieri C FEBS Lett. 2016 Jun 17. doi: 10.1002/1873-3468.12258. PMID:27311405<ref>PMID:27311405</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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<div class="pdbe-citations 4ufq" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
