7e0c: Difference between revisions
New page: '''Unreleased structure''' The entry 7e0c is ON HOLD Authors: Ito, N., Matsuo, S., Inagaki, K., Imada, K. Description: Structure of L-glutamate oxidase R305E mutant [[Category: Unrelea... |
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The | ==Structure of L-glutamate oxidase R305E mutant== | ||
<StructureSection load='7e0c' size='340' side='right'caption='[[7e0c]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7e0c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._X-119-6 Streptomyces sp. X-119-6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E0C 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]] 2.65Å</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></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=7e0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e0c OCA], [https://pdbe.org/7e0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e0c RCSB], [https://www.ebi.ac.uk/pdbsum/7e0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e0c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8L3C7_9ACTN Q8L3C7_9ACTN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The alternation of substrate specificity expands the application range of enzymes in industrial, medical, and pharmaceutical fields. l-Glutamate oxidase (LGOX) from Streptomyces sp. X-119-6 catalyzes the oxidative deamination of l-glutamate to produce 2-ketoglutarate with ammonia and hydrogen peroxide. LGOX shows strict substrate specificity for l-glutamate. Previous studies on LGOX revealed that Arg305 in its active site recognizes the side chain of l-glutamate, and replacement of Arg305 by other amino acids drastically changes the substrate specificity of LGOX. Here we demonstrate that the R305E mutant variant of LGOX exhibits strict specificity for l-arginine. The oxidative deamination activity of LGOX to l-arginine is higher than that of l-arginine oxidase form from Pseudomonas sp. TPU 7192. X-ray crystal structure analysis revealed that the guanidino group of l-arginine is recognized not only by Glu305 but also Asp433, Trp564, and Glu617, which interact with Arg305 in wild-type LGOX. Multiple interactions by these residues provide strict specificity and high activity of LGOX R305E toward l-arginine. LGOX R305E is a thermostable and pH stable enzyme. The amount of hydrogen peroxide, which is a byproduct of oxidative deamination of l-arginine by LGOX R305E, is proportional to the concentration of l-arginine in a range from 0 to 100 muM. The linear relationship is maintained around 1 muM of l-arginine. Thus, LGOX R305E is suitable for the determination of l-arginine. | |||
A new l-arginine oxidase engineered from l-glutamate oxidase.,Yano Y, Matsuo S, Ito N, Tamura T, Kusakabe H, Inagaki K, Imada K Protein Sci. 2021 Mar 25. doi: 10.1002/pro.4070. PMID:33764624<ref>PMID:33764624</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7e0c" style="background-color:#fffaf0;"></div> | ||
[[Category: Inagaki | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces sp. X-119-6]] | |||
[[Category: Imada K]] | |||
[[Category: Inagaki K]] | |||
[[Category: Ito N]] | |||
[[Category: Matsuo S]] | |||
Latest revision as of 19:44, 29 November 2023
Structure of L-glutamate oxidase R305E mutantStructure of L-glutamate oxidase R305E mutant
Structural highlights
FunctionPublication Abstract from PubMedThe alternation of substrate specificity expands the application range of enzymes in industrial, medical, and pharmaceutical fields. l-Glutamate oxidase (LGOX) from Streptomyces sp. X-119-6 catalyzes the oxidative deamination of l-glutamate to produce 2-ketoglutarate with ammonia and hydrogen peroxide. LGOX shows strict substrate specificity for l-glutamate. Previous studies on LGOX revealed that Arg305 in its active site recognizes the side chain of l-glutamate, and replacement of Arg305 by other amino acids drastically changes the substrate specificity of LGOX. Here we demonstrate that the R305E mutant variant of LGOX exhibits strict specificity for l-arginine. The oxidative deamination activity of LGOX to l-arginine is higher than that of l-arginine oxidase form from Pseudomonas sp. TPU 7192. X-ray crystal structure analysis revealed that the guanidino group of l-arginine is recognized not only by Glu305 but also Asp433, Trp564, and Glu617, which interact with Arg305 in wild-type LGOX. Multiple interactions by these residues provide strict specificity and high activity of LGOX R305E toward l-arginine. LGOX R305E is a thermostable and pH stable enzyme. The amount of hydrogen peroxide, which is a byproduct of oxidative deamination of l-arginine by LGOX R305E, is proportional to the concentration of l-arginine in a range from 0 to 100 muM. The linear relationship is maintained around 1 muM of l-arginine. Thus, LGOX R305E is suitable for the determination of l-arginine. A new l-arginine oxidase engineered from l-glutamate oxidase.,Yano Y, Matsuo S, Ito N, Tamura T, Kusakabe H, Inagaki K, Imada K Protein Sci. 2021 Mar 25. doi: 10.1002/pro.4070. PMID:33764624[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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