4e15

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e15]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E15 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e15]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E15 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E15 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SEB:O-BENZYLSULFONYL-SERINE'>SEB</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SEB:O-BENZYLSULFONYL-SERINE'>SEB</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=4e15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e15 OCA], [https://pdbe.org/4e15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e15 RCSB], [https://www.ebi.ac.uk/pdbsum/4e15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e15 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=4e15 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e15 OCA], [https://pdbe.org/4e15 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e15 RCSB], [https://www.ebi.ac.uk/pdbsum/4e15 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e15 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KFA_DROME KFA_DROME]] Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Required for elimination of toxic metabolites.[HAMAP-Rule:MF_03014]<ref>PMID:22690733</ref> <ref>PMID:83140</ref>
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[https://www.uniprot.org/uniprot/KFA_DROME KFA_DROME] Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Required for elimination of toxic metabolites.[HAMAP-Rule:MF_03014]<ref>PMID:22690733</ref> <ref>PMID:83140</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Kynurenine formamidase (KFase), also known as arylformamidase and formylkynurenine formamidase, efficiently catalyzes the hydrolysis of N-formyl-L-kynurenine (NFK) to kynurenine. KFase is the second enzyme in the kynurenine pathway of tryptophan metabolism. A number of intermediates formed in the kynurenine pathway are biologically active and implicated in an assortment of medical conditions, including cancer, schizophrenia and neurodegenerative diseases. Consequently, enzymes involved in the kynurenine pathway have been considered potential regulatory targets. In this study, we report, for the first time, the biochemical characterization and crystal structures of Drosophila melanogaster KFase conjugated with an inhibitor, phenylmethylsulfonyl fluoride (PMSF). The protein architecture of KFase reveals that it belongs to the a/b hydrolase fold family. The PMSF binding information of the solved conjugated crystal structure was used to obtain a KFase and NFK complex using molecular docking. The complex is useful for understanding the catalytic mechanism of KFase. This study provides a molecular basis for future efforts in maintaining or regulating kynurenine metabolism through the molecular and biochemical regulation of KFase.
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Biochemical identification and crystal structure of kynurenine formamidase from Drosophila melanogaster.,Han Q, Robinson H, Li J Biochem J. 2012 Jun 12. PMID:22690733<ref>PMID:22690733</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4e15" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of kynurenine formamidase conjugated with an inhibitor

PDB ID 4e15

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