3ayl

From Proteopedia

(Difference between revisions)

Current revision

X-ray crystal structures of L-phenylalanine oxidase (deaminating and decaboxylating) from Pseudomonas sp. P501. Structures of the enzyme-ligand complex and catalytic mechanism

Structural highlights

3ayl is a 2 chain structure with sequence from Pseudomonas sp. P-501. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.25Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

The mature form of l-Phe oxidase of Pseudomonas sp. P-501 (PAOpt) catalyzes the oxygenative decarboxylation of l-Phe and the oxidative deamination of l-Met, and is highly specific for l-Phe. The crystal structures of PAOpt individually complexed with l-Phe and l-Met and the properties of the active site mutants were investigated to clarify the structural basis of the substrate and reaction specificities of the enzyme. The benzene ring of l-Phe is packed in 6 hydrophobic amino acid side chains versus the 2 hydrophobic side chains of l-amino acid oxidase (LAO, pdb code: 2jb2); the distance between the substrate Calpha atom and water is shorter in the PAOpt- l-Met complex than in the PAOpt-l-Phe complex; and the mutation of substrate carboxylate-binding residues (Arg143 and Tyr536) causes the enzyme to oxidize l-Phe and decreases the charge-transfer band with l-Phe. These results suggest that (1) the higher substrate specificity of PAOpt relative to LAO is derived from the compact hydrophobic nature of the PAOpt active site, and (2) the reactivity of the PAOpt charge-transfer complex with water or oxygen determines whether the enzyme catalyzes oxidation or oxygenation, respectively.

High resolution X-ray crystal structures of L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Structures of the enzyme-ligand complex and catalytic mechanism.,Ida K, Suguro M, Suzuki H J Biochem. 2011 Aug 13. PMID:21841183^[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, Suguro M, Suzuki H. High resolution X-ray crystal structures of L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Structures of the enzyme-ligand complex and catalytic mechanism. J Biochem. 2011 Aug 13. PMID:21841183 doi:10.1093/jb/mvr103

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ayl"

Categories: Large Structures | Pseudomonas sp. P-501 | Suzuki H

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3ayl is ON HOLD
+==X-ray crystal structures of L-phenylalanine oxidase (deaminating and decaboxylating) from Pseudomonas sp. P501. Structures of the enzyme-ligand complex and catalytic mechanism==
+<StructureSection load='3ayl' size='340' side='right'caption='[[3ayl]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3ayl]] 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=3AYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AYL 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]] 1.25&#8491;</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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=3ayl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ayl OCA], [https://pdbe.org/3ayl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ayl RCSB], [https://www.ebi.ac.uk/pdbsum/3ayl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ayl ProSAT]</span></td></tr>
+</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>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The mature form of l-Phe oxidase of Pseudomonas sp. P-501 (PAOpt) catalyzes the oxygenative decarboxylation of l-Phe and the oxidative deamination of l-Met, and is highly specific for l-Phe. The crystal structures of PAOpt individually complexed with l-Phe and l-Met and the properties of the active site mutants were investigated to clarify the structural basis of the substrate and reaction specificities of the enzyme. The benzene ring of l-Phe is packed in 6 hydrophobic amino acid side chains versus the 2 hydrophobic side chains of l-amino acid oxidase (LAO, pdb code: 2jb2); the distance between the substrate Calpha atom and water is shorter in the PAOpt- l-Met complex than in the PAOpt-l-Phe complex; and the mutation of substrate carboxylate-binding residues (Arg143 and Tyr536) causes the enzyme to oxidize l-Phe and decreases the charge-transfer band with l-Phe. These results suggest that (1) the higher substrate specificity of PAOpt relative to LAO is derived from the compact hydrophobic nature of the PAOpt active site, and (2) the reactivity of the PAOpt charge-transfer complex with water or oxygen determines whether the enzyme catalyzes oxidation or oxygenation, respectively.
-Authors: Suzuki, H.
+High resolution X-ray crystal structures of L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. Structures of the enzyme-ligand complex and catalytic mechanism.,Ida K, Suguro M, Suzuki H J Biochem. 2011 Aug 13. PMID:21841183<ref>PMID:21841183</ref>
-Description: X-ray crystal structures of L-phenylalanine oxidase (deaminating and decaboxylating) from Pseudomonas sp. P501. Structures of the enzyme-ligand complex and catalytic mechanism
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3ayl" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Pseudomonas sp. P-501]]
+[[Category: Suzuki H]]

3ayl

From Proteopedia

Current revision

X-ray crystal structures of L-phenylalanine oxidase (deaminating and decaboxylating) from Pseudomonas sp. P501. Structures of the enzyme-ligand complex and catalytic mechanism

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox