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| ==L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813== | | ==L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813== |
| <StructureSection load='3we0' size='340' side='right' caption='[[3we0]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3we0' size='340' side='right'caption='[[3we0]], [[Resolution|resolution]] 1.90Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3we0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Achromobacter_georgiopolitanum Achromobacter georgiopolitanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WE0 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3we0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WE0 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 1.9Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">laao ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Achromobacter georgiopolitanum])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </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=3we0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3we0 OCA], [https://pdbe.org/3we0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3we0 RCSB], [https://www.ebi.ac.uk/pdbsum/3we0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3we0 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=3we0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3we0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3we0 RCSB], [http://www.ebi.ac.uk/pdbsum/3we0 PDBsum]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/B3IVI6_PSEPU B3IVI6_PSEPU] |
| In this study, it was shown for the first time that l-amino acid oxidase of Pseudomonas sp. AIU813, renamed as l-amino acid oxidase/monooxygenase (l-AAO/MOG), exhibits l-lysine 2-monooxygenase as well as oxidase activity. l-Lysine oxidase activity of l-AAO/MOG was increased in a p-chloromercuribenzoate (p-CMB) concentration-dependent manner to a final level that was five fold higher than that of the non-treated enzyme. In order to explain the effects of modification by the sulfhydryl reagent, saturation mutagenesis studies were carried out on five cysteine residues, and we succeeded in identifying l-AAO/MOG C254I mutant enzyme, which showed five-times higher specific activity of oxidase activity than that of wild type. The monooxygenase activity shown by the C254I variant was decreased significantly. Moreover, we also determined a high-resolution three-dimensional structure of l-AAO/MOG to provide a structural basis for its biochemical characteristics. The key residue for the activity conversion of l-AAO/MOG, Cys-254, is located near the aromatic cage (Trp-418, Phe-473, and Trp-516). Although the location of Cys-254 indicates that it is not directly involved in the substrate binding, the chemical modification by p-CMB or C254I mutation would have a significant impact on the substrate binding via the side chain of Trp-516. It is suggested that a slight difference of the binding position of a substrate can dictate the activity of this type of enzyme as oxidase or monooxygenase.
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| Mutational and crystallographic analysis of l-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities.,Matsui D, Im DH, Sugawara A, Fukuta Y, Fushinobu S, Isobe K, Asano Y FEBS Open Bio. 2014 Feb 7;4:220-8. doi: 10.1016/j.fob.2014.02.002. eCollection, 2014. PMID:24693490<ref>PMID:24693490</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| | ==See Also== |
| </div>
| | *[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]] |
| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Achromobacter georgiopolitanum]] | | [[Category: Large Structures]] |
| [[Category: L-amino-acid oxidase]] | | [[Category: Pseudomonas sp]] |
| [[Category: Asano, Y]] | | [[Category: Asano Y]] |
| [[Category: Fukuta, Y]] | | [[Category: Fukuta Y]] |
| [[Category: Fushinobu, S]] | | [[Category: Fushinobu S]] |
| [[Category: Im, D H]] | | [[Category: Im DH]] |
| [[Category: Isobe, K]] | | [[Category: Isobe K]] |
| [[Category: Matsui, D]] | | [[Category: Matsui D]] |
| [[Category: Flavin-containing monoamine oxidase family]]
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| [[Category: Oxidoreductase]]
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| [[Category: Rossmann fold]]
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