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Volumn 123, Issue 6, 1998, Pages 1097-1103

Chemical modification of L-phenylalanine oxidase from Pseudomonas sp. P-501 by phenylglyoxal. Identification of one essential arginyl residue

Author keywords

Active site; Chemical modification; Flavoenzyme; Peptide sequencing; Phenylglyoxal

Indexed keywords

ARGININE; CARBON 14; OXIDOREDUCTASE; PHENYLALANINE; PHENYLGLYOXAL; UNSPECIFIC MONOOXYGENASE;

EID: 0031780907     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022048     Document Type: Article
Times cited : (11)

References (34)
  • 1
    • 0020195726 scopus 로고
    • Purification and characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501
    • Koyama, H. (1982) Purification and characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J. Biochem. 92, 1235-1240
    • (1982) J. Biochem. , vol.92 , pp. 1235-1240
    • Koyama, H.1
  • 2
    • 0020754845 scopus 로고
    • Further characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501
    • Koyama, H. (1983) Further characterization of a novel L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J. Biochem. 93, 1313-1319
    • (1983) J. Biochem. , vol.93 , pp. 1313-1319
    • Koyama, H.1
  • 3
    • 0021478112 scopus 로고
    • Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501
    • Koyama, H. (1984) Oxidation and oxygenation of L-amino acids catalyzed by a L-phenylalanine oxidase (deaminating and decarboxylating) from Pseudomonas sp. P-501. J. Biochem. 96, 421-427
    • (1984) J. Biochem. , vol.96 , pp. 421-427
    • Koyama, H.1
  • 4
    • 0028352155 scopus 로고
    • New subunit in L-phenylalanine oxidase from Pseudomonas sp. P-501 and the primary structure
    • Mukouyama, E.B., Suzuki, H., and Koyama, H. (1994) New subunit in L-phenylalanine oxidase from Pseudomonas sp. P-501 and the primary structure. Arch. Biochem. Biophys. 308, 400-406
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 400-406
    • Mukouyama, E.B.1    Suzuki, H.2    Koyama, H.3
  • 5
    • 33845318295 scopus 로고
    • Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins
    • Wierenga, R.K., De Maeyer, M.C.H., and Hol, W.G.J. (1985) Interaction of pyrophosphate moieties with α-helixes in dinucleotide binding proteins. Biochemistry 24, 1346-1357
    • (1985) Biochemistry , vol.24 , pp. 1346-1357
    • Wierenga, R.K.1    De Maeyer, M.C.H.2    Hol, W.G.J.3
  • 6
    • 0021854287 scopus 로고
    • Regulation of 3-indoleacetic acid production in Pseudomonas syringae pv. savastanoi. Purification and properties of tryptophan 2-monooxygenase
    • Hutcheson, S.W. and Kosuge, T. (1985) Regulation of 3-indoleacetic acid production in Pseudomonas syringae pv. savastanoi. Purification and properties of tryptophan 2-monooxygenase. J. Biol. Chem. 260, 6281-6287
    • (1985) J. Biol. Chem. , vol.260 , pp. 6281-6287
    • Hutcheson, S.W.1    Kosuge, T.2
  • 7
    • 0028984991 scopus 로고
    • Purification and characterization of the flavoprotein tryptophan 2-monooxygenase expressed at high levels in Escherichia coli
    • Emanuele, J.J., Heasley, C.J., and Fitzpatrick, P.F. (1995) Purification and characterization of the flavoprotein tryptophan 2-monooxygenase expressed at high levels in Escherichia coli. Arch. Biochem. Biophys. 316, 241-248
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 241-248
    • Emanuele, J.J.1    Heasley, C.J.2    Fitzpatrick, P.F.3
  • 8
    • 0028902047 scopus 로고
    • Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 1. Kinetic mechanism
    • Emanuele, J.J. and Fitzpatrick, P.F. (1995) Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 1. Kinetic mechanism. Biochemistry 34, 3710-3715
    • (1995) Biochemistry , vol.34 , pp. 3710-3715
    • Emanuele, J.J.1    Fitzpatrick, P.F.2
  • 9
    • 0028949129 scopus 로고
    • Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 2. pH and kinetic isotope effects
    • Emanuele, J.J. and Fitzpatrick, P.F. (1995) Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 2. pH and kinetic isotope effects. Biochemistry 34, 3716-3723
    • (1995) Biochemistry , vol.34 , pp. 3716-3723
    • Emanuele, J.J.1    Fitzpatrick, P.F.2
  • 10
    • 0001793676 scopus 로고
    • D- and L-amino acid oxidases
    • Müller, F., ed. CRC Press, Boca Raton, Ann Arbor, London
    • Curti, B., Ronchi, S., and Simonetta, M.P. (1991) D- and L-amino acid oxidases in Chemistry and Biochemistry of Flavoenzymes (Müller, F., ed.) Vol. III, pp. 69-94, CRC Press, Boca Raton, Ann Arbor, London
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 69-94
    • Curti, B.1    Ronchi, S.2    Simonetta, M.P.3
  • 11
    • 0028234362 scopus 로고
    • Reaction of phenylglyoxal with arginine groups in D-amino-acid oxidase from Rhodotorula gracilis
    • Gadda, G., Negri, A., and Pilone, M.S. (1994) Reaction of phenylglyoxal with arginine groups in D-amino-acid oxidase from Rhodotorula gracilis. J. Biol. Chem. 269, 17809-17814
    • (1994) J. Biol. Chem. , vol.269 , pp. 17809-17814
    • Gadda, G.1    Negri, A.2    Pilone, M.S.3
  • 12
    • 0026563773 scopus 로고
    • Chemical modification of functional arginyl residues in beef kidney D-aspartate oxidase
    • Tedeschi, G., Negri, A., Ceciliani, F., Biondi, P.A., Secchi, C., and Ronchi, S. (1992) Chemical modification of functional arginyl residues in beef kidney D-aspartate oxidase. Eur. J. Biochem. 205, 127-132
    • (1992) Eur. J. Biochem. , vol.205 , pp. 127-132
    • Tedeschi, G.1    Negri, A.2    Ceciliani, F.3    Biondi, P.A.4    Secchi, C.5    Ronchi, S.6
  • 14
  • 15
    • 0025837797 scopus 로고
    • A resonance Raman study on a reaction intermediate of Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating)
    • Suzuki, H., Koyama, H., Nishina, Y., Sato, K., and Shiga, K. (1991) A resonance Raman study on a reaction intermediate of Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating). J. Biochem. 110, 169-172
    • (1991) J. Biochem. , vol.110 , pp. 169-172
    • Suzuki, H.1    Koyama, H.2    Nishina, Y.3    Sato, K.4    Shiga, K.5
  • 16
    • 0014410251 scopus 로고
    • The reaction of phenylglyoxal with arginine residues in proteins
    • Takahashi, K. (1968) The reaction of phenylglyoxal with arginine residues in proteins. J. Biol. Chem. 243, 6171-6179
    • (1968) J. Biol. Chem. , vol.243 , pp. 6171-6179
    • Takahashi, K.1
  • 17
    • 0019276655 scopus 로고
    • Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal
    • Yamasaki, R.B., Vega, A., and Feeney, R.E. (1980) Modification of available arginine residues in proteins by p-hydroxyphenylglyoxal. Anal. Biochem. 109, 32-40
    • (1980) Anal. Biochem. , vol.109 , pp. 32-40
    • Yamasaki, R.B.1    Vega, A.2    Feeney, R.E.3
  • 18
    • 0022798211 scopus 로고
    • Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating)
    • Koyama, H. and Suzuki, H. (1986) Spectral and kinetic studies on Pseudomonas L-phenylalanine oxidase (deaminating and decarboxylating). J. Biochem. 100, 859-866
    • (1986) J. Biochem. , vol.100 , pp. 859-866
    • Koyama, H.1    Suzuki, H.2
  • 19
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Hirs, C.H.W., ed. Academic Press, New York
    • Yang, J.T., Wu, C.-S.C., and Martinez, H.M. (1986) Calculation of protein conformation from circular dichroism in Methods in Enzymology (Hirs, C.H.W., ed.) Vol. 130, pp. 208-269, Academic Press, New York
    • (1986) Methods in Enzymology , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.-S.C.2    Martinez, H.M.3
  • 20
    • 0000399944 scopus 로고
    • Inactivation of myosin by 2,4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds
    • Levy, H.M., Leber, P.D., and Ryan, E.M. (1963) Inactivation of myosin by 2,4-dinitrophenol and protection by adenosine triphosphate and other phosphate compounds. J. Biol. Chem. 238, 3654-3659
    • (1963) J. Biol. Chem. , vol.238 , pp. 3654-3659
    • Levy, H.M.1    Leber, P.D.2    Ryan, E.M.3
  • 21
    • 0029916911 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its new supplement TREMBL
    • Bairoch, A. and Apweiler, R. (1996) The SWISS-PROT protein sequence data bank and its new supplement TREMBL. Nucleic Acids Res. 24, 21-25
    • (1996) Nucleic Acids Res. , vol.24 , pp. 21-25
    • Bairoch, A.1    Apweiler, R.2
  • 23
    • 0026134277 scopus 로고
    • The TR-DNA region carrying the auxin synthesis genes of the Agrobacterium rhizogenes agropine-type plasmid pRiA4: Nucleotide sequence analysis and introduction into tobacco plants
    • Camilleri, C. and Jouanin, L. (1991) The TR-DNA region carrying the auxin synthesis genes of the Agrobacterium rhizogenes agropine-type plasmid pRiA4: nucleotide sequence analysis and introduction into tobacco plants. Mol. Plant Microbe. Interact. 4, 155-162
    • (1991) Mol. Plant Microbe. Interact , vol.4 , pp. 155-162
    • Camilleri, C.1    Jouanin, L.2
  • 24
    • 0026145768 scopus 로고
    • Sequence of Agrobacterium tumefaciens biotype III auxin genes
    • Bonnard, G., Vincent, F., and Otten, L. (1991) Sequence of Agrobacterium tumefaciens biotype III auxin genes. Plant. Mol. Biol. 16, 733-738
    • (1991) Plant. Mol. Biol. , vol.16 , pp. 733-738
    • Bonnard, G.1    Vincent, F.2    Otten, L.3
  • 27
    • 0026677096 scopus 로고
    • Organization and functional analysis of three T-DNAs from the vitopine Ti plasmid pTiS4
    • Canaday, J., Gerard, J.-C., Crouzet, P., and Otten, L. (1992) Organization and functional analysis of three T-DNAs from the vitopine Ti plasmid pTiS4. Mol. Gen. Genet. 235, 292-303
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 292-303
    • Canaday, J.1    Gerard, J.-C.2    Crouzet, P.3    Otten, L.4
  • 28
    • 0022397667 scopus 로고
    • Nucleotide sequences of the Pseudomonas savastanoi indoleacetic acid genes show homology with Agrobacterium tumefaciens T-DNA
    • Yamada, T., Palm, C.J., Brooks, B., and Kosuge, T. (1985) Nucleotide sequences of the Pseudomonas savastanoi indoleacetic acid genes show homology with Agrobacterium tumefaciens T-DNA. Proc. Natl. Acad. Sci. USA 82, 6522-6526
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6522-6526
    • Yamada, T.1    Palm, C.J.2    Brooks, B.3    Kosuge, T.4
  • 29
    • 0025607122 scopus 로고
    • Structure and expression of cDNA for D-amino acid oxidase active against cephalosporin C from Fusarium solani
    • Isogai, T., Ono, H., Ishitani, Y., Kojo, H., Ueda, Y., and Kohsaka, M. (1990) Structure and expression of cDNA for D-amino acid oxidase active against cephalosporin C from Fusarium solani. J. Biochem. 108, 1063-1069
    • (1990) J. Biochem. , vol.108 , pp. 1063-1069
    • Isogai, T.1    Ono, H.2    Ishitani, Y.3    Kojo, H.4    Ueda, Y.5    Kohsaka, M.6
  • 30
    • 0020479451 scopus 로고
    • The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence
    • Ronchi, S., Minchiotti, L., Galliano, M., Curti, B., Swenson, R.P., Williams, C.H. Jr., and Massey, V. (1982) The primary structure of D-amino acid oxidase from pig kidney. II. Isolation and sequence of overlap peptides and the complete sequence. J. Biol. Chem. 257, 8824-8834
    • (1982) J. Biol. Chem. , vol.257 , pp. 8824-8834
    • Ronchi, S.1    Minchiotti, L.2    Galliano, M.3    Curti, B.4    Swenson, R.P.5    Williams Jr., C.H.6    Massey, V.7
  • 31
    • 0023681465 scopus 로고
    • Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase
    • Momoi, K., Fukui, K., Watanabe, F., and Miyake, Y. (1988) Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase. FEBS Lett. 238, 180-184
    • (1988) FEBS Lett. , vol.238 , pp. 180-184
    • Momoi, K.1    Fukui, K.2    Watanabe, F.3    Miyake, Y.4
  • 32
    • 0025120920 scopus 로고
    • Gene expression of D-amino acid oxidase in rabbit kidney
    • Momoi, K., Fukui, K., Tada, M., and Miyake, Y. (1990) Gene expression of D-amino acid oxidase in rabbit kidney. J. Biochem. 108, 406-413
    • (1990) J. Biochem. , vol.108 , pp. 406-413
    • Momoi, K.1    Fukui, K.2    Tada, M.3    Miyake, Y.4
  • 33
    • 0025102689 scopus 로고
    • Cloning and expression of a cDNA encoding mouse kidney D-amino acid oxidase
    • Tada, M., Fukui, K., Momoi, K., and Miyake, Y. (1990) Cloning and expression of a cDNA encoding mouse kidney D-amino acid oxidase. Gene 90, 293-297
    • (1990) Gene , vol.90 , pp. 293-297
    • Tada, M.1    Fukui, K.2    Momoi, K.3    Miyake, Y.4
  • 34
    • 0026651726 scopus 로고
    • The primary structure of the flavoprotein D-aspartate oxidase from beef kidney
    • Negri, A., Ceciliani, F., Tedeschi, G., Simonie, T., and Ronchi, S. (1992) The primary structure of the flavoprotein D-aspartate oxidase from beef kidney. J. Biol. Chem. 267, 11865-11871
    • (1992) J. Biol. Chem. , vol.267 , pp. 11865-11871
    • Negri, A.1    Ceciliani, F.2    Tedeschi, G.3    Simonie, T.4    Ronchi, S.5


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