메뉴 건너뛰기




Volumn 139, Issue 3, 2006, Pages 551-555

Kinetic isotope effect of the L-phenylalanine oxidase from Pseudomonas sp. P-501

Author keywords

Flavoprotein; H tunneling; Kinetic isotope effect; Reductive half reaction; Stopped flow

Indexed keywords

FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; GLYCEROL; METHIONINE; OXIDOREDUCTASE; PHENYLALANINE; PHENYLALANINEOXIDASE; UNCLASSIFIED DRUG;

EID: 33646371735     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvj049     Document Type: Article
Times cited : (8)

References (30)
  • 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
    • 14944361293 scopus 로고    scopus 로고
    • Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme
    • Suzuki, H., Higashi, Y., Asano, M., Suguro, M., Kigawa, M., Maeda, M., Katayama, S., Mukouyama, E.B., and Uchiyama, K. (2004) Sequencing and expression of the L-phenylalanine oxidase gene from Pseudomonas sp. P-501. Proteolytic activation of the proenzyme. J. Biochem. 136, 617-627.
    • (2004) J. Biochem. , vol.136 , pp. 617-627
    • Suzuki, H.1    Higashi, Y.2    Asano, M.3    Suguro, M.4    Kigawa, M.5    Maeda, M.6    Katayama, S.7    Mukouyama, E.B.8    Uchiyama, K.9
  • 5
    • 0028352155 scopus 로고
    • New subunit in L-phenylalanine oxidase from Pseudomonas sp. P-501
    • Mukouyama, E.B., Suzuki, H., and Koyama, H. (1994) New subunit in L-phenylalanine oxidase from Pseudomonas sp. P-501. 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
  • 6
    • 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
  • 7
    • 2042470078 scopus 로고
    • Semiquinone and enzyme kinetics of D-amino acid oxidase
    • Nakamura, T., Nakamura, S., and Ogura, Y. (1963) Semiquinone and enzyme kinetics of D-amino acid oxidase. J. Biochem. 54, 512-519
    • (1963) J. Biochem. , vol.54 , pp. 512-519
    • Nakamura, T.1    Nakamura, S.2    Ogura, Y.3
  • 8
    • 0014983124 scopus 로고
    • Action mechanism of tyramine oxidase from Sarcina lutea
    • Kumagai, H., Yamada, H., Suzuki, H., and Ogura, Y. (1971) Action mechanism of tyramine oxidase from Sarcina lutea. J. Biochem. 69, 137-144
    • (1971) J. Biochem. , vol.69 , pp. 137-144
    • Kumagai, H.1    Yamada, H.2    Suzuki, H.3    Ogura, Y.4
  • 9
    • 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
  • 12
    • 0020989296 scopus 로고
    • On the structures of flavoprotein D-amino acid oxidase purple intermediates. A resonance Raman study
    • Nishina, Y., Shiga, K., Miura, R., Tojo, H., Ohta, M., Miyake, Y., Yamano, T., and Watari, H. (1983) On the structures of flavoprotein D-amino acid oxidase purple intermediates. A resonance Raman study. J. Biochem. 94, 1979-1990
    • (1983) J. Biochem. , vol.94 , pp. 1979-1990
    • Nishina, Y.1    Shiga, K.2    Miura, R.3    Tojo, H.4    Ohta, M.5    Miyake, Y.6    Yamano, T.7    Watari, H.8
  • 13
    • 0017088648 scopus 로고
    • Studies on the reaction specificity of the flavoprotein lysine monooxygenase with modified substrates
    • Ohnishi, T., Yamamoto, S., Hayaishi, O., Izumi, T., and Shiba, T. (1976) Studies on the reaction specificity of the flavoprotein lysine monooxygenase with modified substrates. Arch. Biochem. Biophys. 176, 358-365
    • (1976) Arch. Biochem. Biophys. , vol.176 , pp. 358-365
    • Ohnishi, T.1    Yamamoto, S.2    Hayaishi, O.3    Izumi, T.4    Shiba, T.5
  • 14
    • 0024573393 scopus 로고
    • Hydrogen tunneling in enzyme reactions
    • Cha, Y., Murray, C.J., and Klinman, J.P. (1989) Hydrogen tunneling in enzyme reactions. Science 243, 1325-1330
    • (1989) Science , vol.243 , pp. 1325-1330
    • Cha, Y.1    Murray, C.J.2    Klinman, J.P.3
  • 15
    • 9944236426 scopus 로고    scopus 로고
    • Structural bases of hydrogen tunneling in enzymes: Progress and puzzles
    • Liang, Z.-X. and Klinman, J.P. (2004) Structural bases of hydrogen tunneling in enzymes: progress and puzzles. Curr. Opin. Struc. Biol. 14, 648-655
    • (2004) Curr. Opin. Struc. Biol. , vol.14 , pp. 648-655
    • Liang, Z.-X.1    Klinman, J.P.2
  • 16
    • 0028601412 scopus 로고
    • Hydrogen tunneling in the flavoenzyme monoamine oxidase B
    • Jonsson T., Edmondson D.E., Klinman J.P. (1994) Hydrogen tunneling in the flavoenzyme monoamine oxidase B. Biochemistry 33, 14871-14878
    • (1994) Biochemistry , vol.33 , pp. 14871-14878
    • Jonsson, T.1    Edmondson, D.E.2    Klinman, J.P.3
  • 17
    • 0031025267 scopus 로고    scopus 로고
    • Effect of protein glycosylation on catalysis: Changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction
    • Kohen, A., Jonsson, T., and Klinman, J.P. (1997) Effect of protein glycosylation on catalysis: changes in hydrogen tunneling and enthalpy of activation in the glucose oxidase reaction. Biochemistry 36, 2603-2611
    • (1997) Biochemistry , vol.36 , pp. 2603-2611
    • Kohen, A.1    Jonsson, T.2    Klinman, J.P.3
  • 18
    • 0034673186 scopus 로고    scopus 로고
    • Kinetic studies of the mechanism of carbon-hydrogen bond breakage by the heterotetrameric sarcosine oxidase of Arthrobacter sp. 1-1N
    • Harris, R.J., Meskys, R., Sutcliffe, M.J., and Scrutton, N.S. (2000) Kinetic studies of the mechanism of carbon-hydrogen bond breakage by the heterotetrameric sarcosine oxidase of Arthrobacter sp. 1-1N. Biochemistry 39, 1189-1198
    • (2000) Biochemistry , vol.39 , pp. 1189-1198
    • Harris, R.J.1    Meskys, R.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 19
    • 0035816680 scopus 로고    scopus 로고
    • Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase
    • Basran, J., Sutcliffe, M.J., and Scrutton, N.S. (2001) Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase. J. Biol. Chem. 276, 24581-24587
    • (2001) J. Biol. Chem. , vol.276 , pp. 24581-24587
    • Basran, J.1    Sutcliffe, M.J.2    Scrutton, N.S.3
  • 20
    • 0242582914 scopus 로고    scopus 로고
    • H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase
    • Basran, J., Harris, R.J., Sutcliffe, M.J., and Scrutton, N.S. (2003) H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase. J. Biol. Chem. 278, 43973-43982
    • (2003) J. Biol. Chem. , vol.278 , pp. 43973-43982
    • Basran, J.1    Harris, R.J.2    Sutcliffe, M.J.3    Scrutton, N.S.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0017845014 scopus 로고
    • Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichloro- Phenolindophenol and potassium ferricyanide by L-ascorbic acid
    • Tonomura, B., Nakatani, H., Ohnishi, M., Yamaguchi-Ito, J., and Hitomi, K. (1978) Test reactions for a stopped-flow apparatus. Reduction of 2,6-dichloro- phenolindophenol and potassium ferricyanide by L-ascorbic acid. Anal. Biochem. 84, 370-383
    • (1978) Anal. Biochem. , vol.84 , pp. 370-383
    • Tonomura, B.1    Nakatani, H.2    Ohnishi, M.3    Yamaguchi-Ito, J.4    Hitomi, K.5
  • 23
    • 0029964954 scopus 로고    scopus 로고
    • Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: Implications for enzyme catalysis
    • Jonsson, T., Glickman, M.H., Sun, S., and Klinman, J.P. (1996) Experimental evidence for extensive tunneling of hydrogen in the lipoxygenase reaction: Implications for enzyme catalysis. J. Am. Chem. Soc. 118, 10319-10320
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10319-10320
    • Jonsson, T.1    Glickman, M.H.2    Sun, S.3    Klinman, J.P.4
  • 24
    • 0026707687 scopus 로고
    • Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer
    • Bruno, W.J. and Bialek, W. (1992) Vibrationally enhanced tunneling as a mechanism for enzymatic hydrogen transfer. Biophys. J. 63, 689-699
    • (1992) Biophys. J. , vol.63 , pp. 689-699
    • Bruno, W.J.1    Bialek, W.2
  • 26
    • 0033537697 scopus 로고    scopus 로고
    • Enzymatic H-transfer requires vibration-driven extreme tunneling
    • Basran, J., Sutcliffe, M.J., and Scrutton, N.S. (1999) Enzymatic H-transfer requires vibration-driven extreme tunneling. Biochemistry 38, 3218-3222
    • (1999) Biochemistry , vol.38 , pp. 3218-3222
    • Basran, J.1    Sutcliffe, M.J.2    Scrutton, N.S.3
  • 27
    • 0026636807 scopus 로고
    • The role of solvent viscosity in the dynamics of protein conformational changes
    • Ansari, A., Jones, C.M., Henry, E.R., Hofrichter, J., and Eaton, W.A. (1992) The role of solvent viscosity in the dynamics of protein conformational changes. Science 256, 1796-1798
    • (1992) Science , vol.256 , pp. 1796-1798
    • Ansari, A.1    Jones, C.M.2    Henry, E.R.3    Hofrichter, J.4    Eaton, W.A.5
  • 28
    • 0037035536 scopus 로고    scopus 로고
    • Effect of solution viscosity on intramolecular electron transfer in sulfite oxidase
    • Feng, C., Kedia, R.V., Hazzard, J.T., Hurley, J.K., Tollin, G., and Enemark, J.H. (2002) Effect of solution viscosity on intramolecular electron transfer in sulfite oxidase. Biochemistry 41, 5816-5821
    • (2002) Biochemistry , vol.41 , pp. 5816-5821
    • Feng, C.1    Kedia, R.V.2    Hazzard, J.T.3    Hurley, J.K.4    Tollin, G.5    Enemark, J.H.6
  • 29
    • 0346665918 scopus 로고    scopus 로고
    • Effect of protein dynamics upon reactions that occur in the heme pocket of horseradish peroxidase
    • Khajehlpour, M., Troxlere, T., and Vanderkooi, J.M. (2003) Effect of protein dynamics upon reactions that occur in the heme pocket of horseradish peroxidase. Biochemistry 42, 2672-2679
    • (2003) Biochemistry , vol.42 , pp. 2672-2679
    • Khajehlpour, M.1    Troxlere, T.2    Vanderkooi, J.M.3
  • 30
    • 0035865947 scopus 로고    scopus 로고
    • Viscosity dependence of protein dynamics
    • Walser, R. and van Gunsteren, W.F. (2001) Viscosity dependence of protein dynamics. Proteins 42, 414-421
    • (2001) Proteins , vol.42 , pp. 414-421
    • Walser, R.1    Van Gunsteren, W.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.