2yr4 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.
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.
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
