메뉴 건너뛰기




Volumn 141, Issue 3, 2007, Pages 363-376

Functional and structural characterization of D-aspartate oxidase from porcine kidney: Non-Michaelis kinetics due to substrate activation

Author keywords

cDNA cloning; D aspartate; D aspartate oxidase; Neuroendocrine system; Porcine kidney

Indexed keywords

ASPARTATE OXIDASE; COMPLEMENTARY DNA; DEXTRO ASPARTIC ACID; DEXTRO GLUTAMIC ACID; DICARBOXYLIC ACID DERIVATIVE; FLAVINE ADENINE NUCLEOTIDE; N METHYL DEXTRO ASPARTIC ACID; TARTARIC ACID; TETRAMER;

EID: 34248647913     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvm041     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 0030850891 scopus 로고    scopus 로고
    • Free D-aspartate and D-serine in the mammalian brain and periphery
    • Hashimoto, A. and Oka, T. (1997) Free D-aspartate and D-serine in the mammalian brain and periphery. Progr. Neurobiol. 52, 325-353
    • (1997) Progr. Neurobiol , vol.52 , pp. 325-353
    • Hashimoto, A.1    Oka, T.2
  • 2
    • 0031043465 scopus 로고    scopus 로고
    • Schell, M.J., Cooper, O.B., and Snyder, S.H. (1997) D-aspartate localizations imply neuronal and neuroendocrine roles. Proc. Natl. Acad. Sci. USA 94, 2013-2018
    • Schell, M.J., Cooper, O.B., and Snyder, S.H. (1997) D-aspartate localizations imply neuronal and neuroendocrine roles. Proc. Natl. Acad. Sci. USA 94, 2013-2018
  • 3
    • 0033554262 scopus 로고    scopus 로고
    • Lee, J.-A., Homma, H., Tashiro, K., Iwatsubo, T., and Imai, K. (1999) D-Aspartate localization in the rat pituitary gland and retina. Brain Res. 838, 193-199
    • Lee, J.-A., Homma, H., Tashiro, K., Iwatsubo, T., and Imai, K. (1999) D-Aspartate localization in the rat pituitary gland and retina. Brain Res. 838, 193-199
  • 4
    • 0034618848 scopus 로고    scopus 로고
    • Wolosker, H., D'Aniello, A., and Snyder, S.H. (2000) D-Aspartate disposition in neuronal and endocrine tissues: ontogeny, biosynthesis and release. Neuroscience 100, 183-189
    • Wolosker, H., D'Aniello, A., and Snyder, S.H. (2000) D-Aspartate disposition in neuronal and endocrine tissues: ontogeny, biosynthesis and release. Neuroscience 100, 183-189
  • 5
    • 0034077625 scopus 로고    scopus 로고
    • Occurrence of D-aspartic acid and N-methyl-D-aspartic acid in rat neuroendocrine tissues and their role in the modulation of luteinizing hormone and growth hormone release
    • D'Aniello, A., Di Fiore, M.M., Fisher, G.H., Milone, A., Seleni, A., D'Aniello, S., Perna, A.F., and Ingrosso, D. (2000) Occurrence of D-aspartic acid and N-methyl-D-aspartic acid in rat neuroendocrine tissues and their role in the modulation of luteinizing hormone and growth hormone release. FASEB J. 14, 699-714
    • (2000) FASEB J , vol.14 , pp. 699-714
    • D'Aniello, A.1    Di Fiore, M.M.2    Fisher, G.H.3    Milone, A.4    Seleni, A.5    D'Aniello, S.6    Perna, A.F.7    Ingrosso, D.8
  • 6
    • 0037126987 scopus 로고    scopus 로고
    • Naturally occurring free D-aspartate is a nuclear component of cells in the mammalian hypothalamo-neurohypophyseal system
    • Wang, H., Wolosker, H., Morris, J.F., Pevsner, J., Snyder, S.H., and Selkoe, D.J. (2002) Naturally occurring free D-aspartate is a nuclear component of cells in the mammalian hypothalamo-neurohypophyseal system. Neuroscience 109, 1-4
    • (2002) Neuroscience , vol.109 , pp. 1-4
    • Wang, H.1    Wolosker, H.2    Morris, J.F.3    Pevsner, J.4    Snyder, S.H.5    Selkoe, D.J.6
  • 7
    • 33845245430 scopus 로고    scopus 로고
    • Biochemistry of D-aspartate in mammalian cells
    • Homma, H. (2007) Biochemistry of D-aspartate in mammalian cells. Amino Acids 32, 3-11
    • (2007) Amino Acids , vol.32 , pp. 3-11
    • Homma, H.1
  • 8
    • 0032581422 scopus 로고    scopus 로고
    • Takigawa, Y., Homma, H., Lee, J.-A., Fukushima, T., Santa, T., Iwatsubo, T., and Imai, K. (1998) D-Aspartate uptake into cultured rat pinealocytes and the concomitant effect on L-asparate levels and melatonin secretion. Biochem. Biophys. Res. Commun. 248, 641-647
    • Takigawa, Y., Homma, H., Lee, J.-A., Fukushima, T., Santa, T., Iwatsubo, T., and Imai, K. (1998) D-Aspartate uptake into cultured rat pinealocytes and the concomitant effect on L-asparate levels and melatonin secretion. Biochem. Biophys. Res. Commun. 248, 641-647
  • 9
    • 0034610020 scopus 로고    scopus 로고
    • 3). Biochem. Biophys. Res. Commun. 276, 1143-1147
    • 3). Biochem. Biophys. Res. Commun. 276, 1143-1147
  • 10
    • 0033735457 scopus 로고    scopus 로고
    • The role of D-aspartic acid and N-methyl-D-aspartic acid in the regulation of prolactin release
    • D'Aniello, G., Tolino, A., D'Aniello, A., Errico, F., Fisher, G.H., and Di Fiore, M.M. (2000) The role of D-aspartic acid and N-methyl-D-aspartic acid in the regulation of prolactin release. Endocrinology 141, 3862-3870
    • (2000) Endocrinology , vol.141 , pp. 3862-3870
    • D'Aniello, G.1    Tolino, A.2    D'Aniello, A.3    Errico, F.4    Fisher, G.H.5    Di Fiore, M.M.6
  • 11
    • 0033781495 scopus 로고    scopus 로고
    • Regulation of rat magnocellular neuro-secretory system by D-aspartate: Evidence for biological role(s) of a naturally occurring free D-amino acid in mammals
    • Wang, H., Wolosker, H., Pevsner, J., Synder, S.H., and Selkoe, D.J. (2000) Regulation of rat magnocellular neuro-secretory system by D-aspartate: evidence for biological role(s) of a naturally occurring free D-amino acid in mammals. J. Endocrinol. 167, 247-252
    • (2000) J. Endocrinol , vol.167 , pp. 247-252
    • Wang, H.1    Wolosker, H.2    Pevsner, J.3    Synder, S.H.4    Selkoe, D.J.5
  • 12
    • 0035854808 scopus 로고    scopus 로고
    • 2+-dependent pathway in a subset of rat pheochromocytoma PC12 cells. J. Biol. Chem. 276, 26589-26596
    • 2+-dependent pathway in a subset of rat pheochromocytoma PC12 cells. J. Biol. Chem. 276, 26589-26596
  • 13
    • 33644824256 scopus 로고    scopus 로고
    • Huang, A.S., Beigneux, A., Weil, Z.M., Kim, P.M., Molliver, M.E., Blackshaw, S., Nelson, R.J., Young, S.G., and Snyder, S.H. (2006) D-Aspartate regulates melanocortin formation and function: behavioral alterations in D-aspartate oxidase-deficient mice. J. Neurosci. 26, 2814-2819
    • Huang, A.S., Beigneux, A., Weil, Z.M., Kim, P.M., Molliver, M.E., Blackshaw, S., Nelson, R.J., Young, S.G., and Snyder, S.H. (2006) D-Aspartate regulates melanocortin formation and function: behavioral alterations in D-aspartate oxidase-deficient mice. J. Neurosci. 26, 2814-2819
  • 14
    • 33746196730 scopus 로고    scopus 로고
    • A physiological mechanism to regulate D-aspartic acid and NMDA levels in mammals reveled by D-aspartate oxidase deficient mice
    • Errico, F., Pirro, M.T., Affuso, A., Spinelli, P., De Felice, M., D'Aniello, A., and Di Lauro, R. (2006) A physiological mechanism to regulate D-aspartic acid and NMDA levels in mammals reveled by D-aspartate oxidase deficient mice. Gene 374, 50-57
    • (2006) Gene , vol.374 , pp. 50-57
    • Errico, F.1    Pirro, M.T.2    Affuso, A.3    Spinelli, P.4    De Felice, M.5    D'Aniello, A.6    Di Lauro, R.7
  • 16
    • 0023664644 scopus 로고    scopus 로고
    • Negri, A., Massey, V., and Williams, Jr., C.H. (1987) D-Aspartate oxidase from beef kidney. Purification and properties. J. Biol. Chem. 262, 10026-10034
    • Negri, A., Massey, V., and Williams, Jr., C.H. (1987) D-Aspartate oxidase from beef kidney. Purification and properties. J. Biol. Chem. 262, 10026-10034
  • 17
    • 0014223130 scopus 로고    scopus 로고
    • De Marco, C. and Crifo, C. (1967) D-Aspartate oxidase from pig kidney. 3. Competitive inhibition by dicarboxylic hydroxyacids. Enzymologia 33, 325-330
    • De Marco, C. and Crifo, C. (1967) D-Aspartate oxidase from pig kidney. 3. Competitive inhibition by dicarboxylic hydroxyacids. Enzymologia 33, 325-330
  • 18
    • 0016591855 scopus 로고    scopus 로고
    • Jaroszewicz, L. (1975) D-Aspartate oxidase in the thyroid gland. Enzyme 20, 80-89
    • Jaroszewicz, L. (1975) D-Aspartate oxidase in the thyroid gland. Enzyme 20, 80-89
  • 19
    • 0030892155 scopus 로고    scopus 로고
    • Structural and functional characterization of the human brain D-aspartate oxidase
    • Setoyama, C. and Miura, R. (1997) Structural and functional characterization of the human brain D-aspartate oxidase. J. Biochem. 121, 798-803
    • (1997) J. Biochem , vol.121 , pp. 798-803
    • Setoyama, C.1    Miura, R.2
  • 20
    • 0030936716 scopus 로고    scopus 로고
    • cDNA cloning and expression of the flavoprotein D-aspartate oxidase from bovine kidney cortex
    • Simonic, T., Duga, S., Negri, A., Tedeschi, G., Malcovati, M., Tenchini, M.L., and Ronchi, S. (1997) cDNA cloning and expression of the flavoprotein D-aspartate oxidase from bovine kidney cortex. Biochem. J. 322, 729-735
    • (1997) Biochem. J , vol.322 , pp. 729-735
    • Simonic, T.1    Duga, S.2    Negri, A.3    Tedeschi, G.4    Malcovati, M.5    Tenchini, M.L.6    Ronchi, S.7
  • 21
    • 0032913359 scopus 로고    scopus 로고
    • Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors
    • Negri, A., Tedeschi, G., Ceciliani, F., and Ronchi, S. (1999) Purification of beef kidney D-aspartate oxidase overexpressed in Escherichia coli and characterization of its redox potentials and oxidative activity towards agonists and antagonists of excitatory amino acid receptors. Biochim. Biophys. Acta 1431, 212-222
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 212-222
    • Negri, A.1    Tedeschi, G.2    Ceciliani, F.3    Ronchi, S.4
  • 22
    • 33845239217 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA encoding mouse D-aspartate oxidase and functional characterization of its recombinant proteins by site-directed mutagenesis
    • Katane, M., Furuchi, T., Sekine, M., and Homma, H. (2007) Molecular cloning of a cDNA encoding mouse D-aspartate oxidase and functional characterization of its recombinant proteins by site-directed mutagenesis. Amino Acids 32, 69-78
    • (2007) Amino Acids , vol.32 , pp. 69-78
    • Katane, M.1    Furuchi, T.2    Sekine, M.3    Homma, H.4
  • 23
    • 0023737116 scopus 로고
    • The kinetic mechanism of beef kidney D-aspartate oxidase
    • Negri, A., Massey, V., Williams, Jr., C.H. and Schopfer, L.M. (1988) The kinetic mechanism of beef kidney D-aspartate oxidase. J. Biol. Chem. 263, 13557-13563
    • (1988) J. Biol. Chem , vol.263 , pp. 13557-13563
    • Negri, A.1    Massey, V.2    Williams Jr., C.H.3    Schopfer, L.M.4
  • 24
    • 0019921265 scopus 로고
    • The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase
    • Nasu, S., Wicks, F.D., and Gholson, R.K. (1982) The mammalian enzyme which replaces B protein of E. coli quinolinate synthetase is D-aspartate oxidase. Biochim. Biophys. Acta 704, 240-252
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 240-252
    • Nasu, S.1    Wicks, F.D.2    Gholson, R.K.3
  • 25
    • 0021778413 scopus 로고    scopus 로고
    • Hamilton, G.A. (1985) Peroxisomal oxidases and suggestions for the mechanism of action of insulin and other hormones in Advances in Enzymology (Meister, A., ed.) 57, pp. 85-178, John Wiley & Sons, New York
    • Hamilton, G.A. (1985) Peroxisomal oxidases and suggestions for the mechanism of action of insulin and other hormones in Advances in Enzymology (Meister, A., ed.) Vol. 57, pp. 85-178, John Wiley & Sons, New York
  • 26
    • 0033930404 scopus 로고    scopus 로고
    • Three-dimensional structure of the purple intermediate of porcine kidney D-amino acid oxidase. Optimization of the oxidative half-reaction through alignment of the product with reduced flavin
    • Mizutani, H., Miyahara, I., Hirotsu, K., Nishina, Y., Shiga, K., Setoyama, C., and Miura, R. (2000) Three-dimensional structure of the purple intermediate of porcine kidney D-amino acid oxidase. Optimization of the oxidative half-reaction through alignment of the product with reduced flavin. J. Biochem. 128, 73-81
    • (2000) J. Biochem , vol.128 , pp. 73-81
    • Mizutani, H.1    Miyahara, I.2    Hirotsu, K.3    Nishina, Y.4    Shiga, K.5    Setoyama, C.6    Miura, R.7
  • 27
    • 0035719831 scopus 로고    scopus 로고
    • pH and kinetic isotope effects in D-amino acid oxidase catalysis. Evidence for a concerted mechanism in substrate dehydrogenation via hydride transfer
    • Harris, C.M., Pollegioni, L., and Ghisla, S. (2001) pH and kinetic isotope effects in D-amino acid oxidase catalysis. Evidence for a concerted mechanism in substrate dehydrogenation via hydride transfer. Eur. J. Biochem. 268, 5504-5520
    • (2001) Eur. J. Biochem , vol.268 , pp. 5504-5520
    • Harris, C.M.1    Pollegioni, L.2    Ghisla, S.3
  • 29
    • 0036242051 scopus 로고    scopus 로고
    • Accurate measurement of near-micromolar oxygen concentrations in aqueous solutions based on enzymatic extradiol cleavage of 4-chlorocatechol: Application to improved low-oxygen experimental systems and quantitative assessment of back diffusion of oxygen from the atmosphere
    • Nakajima, H., Ishida, T., Tanaka, H., and Horiike, K. (2002) Accurate measurement of near-micromolar oxygen concentrations in aqueous solutions based on enzymatic extradiol cleavage of 4-chlorocatechol: application to improved low-oxygen experimental systems and quantitative assessment of back diffusion of oxygen from the atmosphere. J. Biochem. 131, 523-531
    • (2002) J. Biochem , vol.131 , pp. 523-531
    • Nakajima, H.1    Ishida, T.2    Tanaka, H.3    Horiike, K.4
  • 30
    • 33846655347 scopus 로고    scopus 로고
    • Simultaneous measurement of D-serine dehydratase and D-amino acid oxidase activities by the detection of 2-oxo-acid formation with reverse-phase HPLC
    • doi:10.1016/j.ab.2006.12.025
    • Tanaka, H., Yamamoto, A., Ishida, T., and Horiike, K. (2007) Simultaneous measurement of D-serine dehydratase and D-amino acid oxidase activities by the detection of 2-oxo-acid formation with reverse-phase HPLC. Anal. Biochem. doi:10.1016/j.ab.2006.12.025
    • (2007) Anal. Biochem
    • Tanaka, H.1    Yamamoto, A.2    Ishida, T.3    Horiike, K.4
  • 31
    • 0000171230 scopus 로고
    • A new method for preparing flavin-adenine dinucleotide
    • Whitby, L.G. (1953) A new method for preparing flavin-adenine dinucleotide. Biochem. J. 54, 437-442
    • (1953) Biochem. J , vol.54 , pp. 437-442
    • Whitby, L.G.1
  • 32
    • 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
  • 33
    • 0035054006 scopus 로고    scopus 로고
    • Purification and characterization of homo- and heterodimeric acetate kinases from the sulfate-reducing bacterium Desulfovibrio vulgaris
    • Yu, L., Ishida, T., Ozawa, K., Akutsu, H., and Horiike, K. (2001) Purification and characterization of homo- and heterodimeric acetate kinases from the sulfate-reducing bacterium Desulfovibrio vulgaris. J. Biochem. 129, 411-421
    • (2001) J. Biochem , vol.129 , pp. 411-421
    • Yu, L.1    Ishida, T.2    Ozawa, K.3    Akutsu, H.4    Horiike, K.5
  • 34
    • 0028988356 scopus 로고
    • Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered Escherichia coli
    • Kobayashi, T., Ishida, T., Horiike, K., Takahara, Y., Numao, N., Nakazawa, A., Nakazawa, T., and Nozaki, M. (1995) Overexpression of Pseudomonas putida catechol 2,3-dioxygenase with high specific activity by genetically engineered Escherichia coli. J. Biochem. 117, 614-622
    • (1995) J. Biochem , vol.117 , pp. 614-622
    • Kobayashi, T.1    Ishida, T.2    Horiike, K.3    Takahara, Y.4    Numao, N.5    Nakazawa, A.6    Nakazawa, T.7    Nozaki, M.8
  • 37
    • 0033741877 scopus 로고    scopus 로고
    • The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation
    • Umhau, S., Pollegioni, L., Molla, G., Diederichs, K., Welte, W., Pilone, M.S., and Ghisla, S. (2000) The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation. Proc. Natl. Acad. Sci. USA 97, 12463-12468
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12463-12468
    • Umhau, S.1    Pollegioni, L.2    Molla, G.3    Diederichs, K.4    Welte, W.5    Pilone, M.S.6    Ghisla, S.7
  • 38
    • 33745738478 scopus 로고    scopus 로고
    • Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the "active-site lid
    • Setoyama, C., Nishina, Y., Mizutani, H., Miyahara, I., Hirotsu, K., Kamiya, N., Shiga, K., and Miura, R. (2006) Engineering the substrate specificity of porcine kidney D-amino acid oxidase by mutagenesis of the "active-site lid". J. Biochem. 139, 873-879
    • (2006) J. Biochem , vol.139 , pp. 873-879
    • Setoyama, C.1    Nishina, Y.2    Mizutani, H.3    Miyahara, I.4    Hirotsu, K.5    Kamiya, N.6    Shiga, K.7    Miura, R.8
  • 39
    • 0020080252 scopus 로고    scopus 로고
    • Nasu, S., Wicks, F.D., and Gholson, R.K. (1982) L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase. J. Biol. Chem. 257, 626-632
    • Nasu, S., Wicks, F.D., and Gholson, R.K. (1982) L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase. J. Biol. Chem. 257, 626-632
  • 40
    • 0037022788 scopus 로고    scopus 로고
    • Structure of FAD-bound L-aspartate oxidase: Insight into substrate specificity and catalysis
    • Bossi, R.T., Negri, A., Tedeschi, G., and Mattevi, A. (2002) Structure of FAD-bound L-aspartate oxidase: Insight into substrate specificity and catalysis. Biochemistry 41, 3018-3024
    • (2002) Biochemistry , vol.41 , pp. 3018-3024
    • Bossi, R.T.1    Negri, A.2    Tedeschi, G.3    Mattevi, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.