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| | <StructureSection load='2yr6' size='340' side='right'caption='[[2yr6]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='2yr6' size='340' side='right'caption='[[2yr6]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yr6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp._p-501 Pseudomonas sp. p-501]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YR6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YR6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2yr6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._P-501 Pseudomonas sp. P-501]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YR6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2yr4|2yr4]], [[2yr5|2yr5]], [[2yr7|2yr7]], [[2yr8|2yr8]], [[2yr9|2yr9]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BE2:2-AMINOBENZOIC+ACID'>BE2</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylalanine_2-monooxygenase Phenylalanine 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.9 1.13.12.9] </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=2yr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yr6 OCA], [https://pdbe.org/2yr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yr6 RCSB], [https://www.ebi.ac.uk/pdbsum/2yr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yr6 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2yr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yr6 OCA], [http://pdbe.org/2yr6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yr6 RCSB], [http://www.ebi.ac.uk/pdbsum/2yr6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yr6 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PAO_PSESP PAO_PSESP] Catalyzes both oxygenative decarboxylation and oxidative deamination, depending on the substrate used. Has high activity for L-Phe and L-Tyr, but relatively low activities for L-Met and L-Trp. L-Phe is mainly oxygenated and L-Met is mainly oxidized.<ref>PMID:15632301</ref> <ref>PMID:16567420</ref> <ref>PMID:3818566</ref> <ref>PMID:6501250</ref> <ref>PMID:6885723</ref> <ref>PMID:7174643</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phenylalanine 2-monooxygenase]]
| + | [[Category: Pseudomonas sp. P-501]] |
| - | [[Category: Pseudomonas sp. p-501]] | + | [[Category: Ida K]] |
| - | [[Category: Ida, K]] | + | [[Category: Kurabayashi M]] |
| - | [[Category: Kurabayashi, M]] | + | [[Category: Suguro M]] |
| - | [[Category: Suguro, M]] | + | [[Category: Suzuki H]] |
| - | [[Category: Suzuki, H]] | + | |
| - | [[Category: Amino oxidase]]
| + | |
| - | [[Category: Flavoenzyme]]
| + | |
| - | [[Category: L-phenylalanine oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
PAO_PSESP Catalyzes both oxygenative decarboxylation and oxidative deamination, depending on the substrate used. Has high activity for L-Phe and L-Tyr, but relatively low activities for L-Met and L-Trp. L-Phe is mainly oxygenated and L-Met is mainly oxidized.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The mature form of l-phenylalanine oxidase (PAOpt) from Pseudomonas sp. P-501 was generated and activated by the proteolytic cleavage of a noncatalytic proenzyme (proPAO). The crystal structures of proPAO, PAOpt, and the PAOpt-o-amino benzoate (AB) complex were determined at 1.7, 1.25, and 1.35A resolutions, respectively. The structure of proPAO suggests that the prosequence peptide of proPAO occupies the funnel (pathway) of the substrate amino acid from the outside of the protein to the interior flavin ring, whereas the funnel is closed with the hydrophobic residues at its vestibule in both PAOpt and the PAOpt-AB complex. All three structures have an oxygen channel that is open to the surface of the protein from the flavin ring. These results suggest that structural changes were induced by proteolysis; that is, the proteolysis of proPAO removes the prosequence and closes the funnel to keep the active site hydrophobic but keeps the oxygen channel open. The possibility that an interaction of the hydrophobic side chain of substrate with the residues of the vestibule region may open the funnel as a putative amino acid channel is discussed.
Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501.,Ida K, Kurabayashi M, Suguro M, Hiruma Y, Hikima T, Yamomoto M, Suzuki H J Biol Chem. 2008 Jun 13;283(24):16584-90. doi: 10.1074/jbc.M800366200. Epub 2008, Apr 16. PMID:18417467[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Suzuki H, Higashi Y, Asano M, Suguro M, Kigawa M, Maeda M, Katayama S, Mukouyama EB, Uchiyama K. Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme. J Biochem. 2004 Nov;136(5):617-27. PMID:15632301 doi:10.1093/jb/mvh169
- ↑ Ohta Y, Mukouyama EB, Suzuki H. Kinetic isotope effect of the L-phenylalanine oxidase from Pseudomonas sp. P-501. J Biochem. 2006 Mar;139(3):551-5. PMID:16567420 doi:10.1093/jb/mvj049
- ↑ Koyama H, Suzuki H. Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating). J Biochem. 1986 Oct;100(4):859-66. PMID:3818566 doi:10.1093/oxfordjournals.jbchem.a121798
- ↑ Koyama H. Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1984 Aug;96(2):421-7. PMID:6501250 doi:10.1093/oxfordjournals.jbchem.a134853
- ↑ Koyama H. Further characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1983 May;93(5):1313-9. PMID:6885723 doi:10.1093/oxfordjournals.jbchem.a134265
- ↑ Koyama H. Purification and characterization of a novel L-phenylalanine oxidase (Deaminating and decarboxylating) from Pseudomonas sp. P-501. J Biochem. 1982 Oct;92(4):1235-40. PMID:7174643 doi:10.1093/oxfordjournals.jbchem.a134041
- ↑ Ida K, Kurabayashi M, Suguro M, Hiruma Y, Hikima T, Yamomoto M, Suzuki H. Structural basis of proteolytic activation of L-phenylalanine oxidase from Pseudomonas sp. P-501. J Biol Chem. 2008 Jun 13;283(24):16584-90. doi: 10.1074/jbc.M800366200. Epub 2008, Apr 16. PMID:18417467 doi:http://dx.doi.org/10.1074/jbc.M800366200
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