View source for 8bmu


==Engineered Fructosyl Peptide Oxidase - X04 mutant==
<StructureSection load='8bmu' size='340' side='right'caption='[[8bmu]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8bmu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Parastagonospora_nodorum_SN15 Parastagonospora nodorum SN15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BMU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BMU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=8bmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bmu OCA], [https://pdbe.org/8bmu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bmu RCSB], [https://www.ebi.ac.uk/pdbsum/8bmu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bmu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0UIL6_PHANO Q0UIL6_PHANO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fructosyl peptide oxidases (FPOX) are deglycating enzymes that find application as key enzymatic components in diabetes monitoring devices. Indeed, their use with blood samples can provide a measurement of the concentration of glycated hemoglobin and glycated albumin, two well-known diabetes markers. However, the FPOX currently employed in enzymatic assays cannot directly detect whole glycated proteins, making it necessary to perform a preliminary proteolytic treatment of the target protein to generate small glycated peptides that can act as viable substrates for the enzyme. This is a costly and time consuming step. In this work, we used an in silico protein engineering approach to enhance the overall thermal stability of the enzyme and to improve its catalytic activity toward large substrates. The final design shows a marked improvement in thermal stability relative to the wild type enzyme, a distinct widening of its access tunnel and significant enzymatic activity towards a range of glycated substrates.

Tailoring FPOX enzymes for enhanced stability and expanded substrate recognition.,Estiri H, Bhattacharya S, Buitrago JAR, Castagna R, Legzdina L, Casucci G, Ricci A, Parisini E, Gautieri A Sci Rep. 2023 Oct 30;13(1):18610. doi: 10.1038/s41598-023-45428-1. PMID:37903872<ref>PMID:37903872</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8bmu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Parastagonospora nodorum SN15]]
[[Category: Bhattacharya S]]
[[Category: Estiri H]]
[[Category: Parisini E]]
[[Category: Rodriguez-Buitrago JA]]