3we0: Difference between revisions
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== 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 [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> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>< | </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> | ||
<tr><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='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><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='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><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> | <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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Achromobacter georgiopolitanum]] | [[Category: Achromobacter georgiopolitanum]] | ||
[[Category: L-amino-acid oxidase]] | [[Category: L-amino-acid oxidase]] | ||
[[Category: Asano, Y | [[Category: Asano, Y]] | ||
[[Category: Fukuta, Y | [[Category: Fukuta, Y]] | ||
[[Category: Fushinobu, S | [[Category: Fushinobu, S]] | ||
[[Category: Im, D H | [[Category: Im, D H]] | ||
[[Category: Isobe, K | [[Category: Isobe, K]] | ||
[[Category: Matsui, D | [[Category: Matsui, D]] | ||
[[Category: Flavin-containing monoamine oxidase family]] | [[Category: Flavin-containing monoamine oxidase family]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 12:54, 4 January 2015
L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813
Structural highlights
Publication Abstract from PubMedIn 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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