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| | ==Crystal structure of A. niger ochratoxinase== | | ==Crystal structure of A. niger ochratoxinase== |
| - | <StructureSection load='4c5y' size='340' side='right' caption='[[4c5y]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4c5y' size='340' side='right'caption='[[4c5y]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4c5y]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/A._niger A. niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C5Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4c5y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C5Y FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c5z|4c5z]], [[4c60|4c60]], [[4c65|4c65]]</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=4c5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5y OCA], [https://pdbe.org/4c5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c5y RCSB], [https://www.ebi.ac.uk/pdbsum/4c5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5y ProSAT]</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=4c5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c5y OCA], [http://pdbe.org/4c5y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c5y RCSB], [http://www.ebi.ac.uk/pdbsum/4c5y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c5y ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OTASE_ASPNC OTASE_ASPNC] Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products (PubMed:24947135).<ref>PMID:24947135</ref> <ref>PMID:33647354</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: A. niger]] | + | [[Category: Aspergillus niger]] |
| - | [[Category: Dobritzsch, D]] | + | [[Category: Large Structures]] |
| - | [[Category: Schneider, G]] | + | [[Category: Dobritzsch D]] |
| - | [[Category: Wang, H]] | + | [[Category: Schneider G]] |
| - | [[Category: Yu, S]] | + | [[Category: Wang H]] |
| - | [[Category: Amidohydrolase superfamily]]
| + | [[Category: Yu S]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Metal-dependent amidohydrolase]]
| + | |
| - | [[Category: Ochratoxin a hydrolysis]]
| + | |
| Structural highlights
Function
OTASE_ASPNC Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products (PubMed:24947135).[1] [2]
Publication Abstract from PubMed
Ochratoxin, with ochratoxin A as the dominant form, is one of the five major mycotoxins most harmful to humans and animals. It is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products. Detoxification of contaminated food is a challenging health issue. Here we report the identification, characterization and crystal structure (at 2.2 A) of a novel, microbial ochratoxinase from Aspergillus niger. A putative amidase gene encoding a 480 amino acid polypeptide was cloned and homologously expressed in A. niger. The recombinant protein is N-terminally truncated, thermostable, has optimal activity at pH~6 and 66 degrees C, and is more efficient in ochratoxin A hydrolysis than carboxypeptidase A and Y, the two previously known enzymes capable of degrading this mycotoxin. The subunit of the homooctameric enzyme folds into a two-domain structure characteristic for a metal dependent amidohydrolase, with a twisted TIM-barrel and a smaller b-sandwich domain. The active site contains an aspartate residue for acid-base catalysis, and a carboxylated lysine and four histidine residues for binding of a binuclear metal center.
Structural and functional characterization of ochratoxinase, a novel mycotoxin degrading enzyme.,Dobritzsch D, Wang H, Schneider G, Yu S Biochem J. 2014 Jun 20. PMID:24947135[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dobritzsch D, Wang H, Schneider G, Yu S. Structural and functional characterization of ochratoxinase, a novel mycotoxin degrading enzyme. Biochem J. 2014 Jun 20. PMID:24947135 doi:http://dx.doi.org/10.1042/BJ20140382
- ↑ Xiong K, Liu J, Wang X, Sun B, Zhang Y, Zhao Z, Pei P, Li X. Engineering a carboxypeptidase from Aspergillus niger M00988 by mutation to increase its ability in high Fischer ratio oligopeptide preparation. J Biotechnol. 2021 Mar 20;330:1-8. doi: 10.1016/j.jbiotec.2021.02.015. Epub 2021 , Feb 26. PMID:33647354 doi:http://dx.doi.org/10.1016/j.jbiotec.2021.02.015
- ↑ Dobritzsch D, Wang H, Schneider G, Yu S. Structural and functional characterization of ochratoxinase, a novel mycotoxin degrading enzyme. Biochem J. 2014 Jun 20. PMID:24947135 doi:http://dx.doi.org/10.1042/BJ20140382
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