메뉴 건너뛰기




Volumn 239, Issue 2, 1996, Pages 427-433

L-Aspartate oxidase from Escherichia coli - II. Interaction with C4 dicarboxylic acids and identification of a novel L-aspartate:fumarate oxidoreductase activity

Author keywords

FAD; Flavoprotein; Fumarate reductase; L aspartate oxidase; Photoreduction

Indexed keywords

DICARBOXYLIC ACID; FLAVOPROTEIN; FUMARATE REDUCTASE; FUMARIC ACID; OXIDOREDUCTASE; PYRIDINE NUCLEOTIDE; SUCCINIC ACID; SULFITE;

EID: 0030037614     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0427u.x     Document Type: Article
Times cited : (50)

References (18)
  • 1
    • 0020080252 scopus 로고
    • L-Aspartate oxidase, a newly discovered enzyme of Escherichia coli, is the B protein of quinolinate synthetase
    • Nasu, S., Wicks, F. D. & 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.
    • (1982) J. Biol. Chem. , vol.257 , pp. 626-632
    • Nasu, S.1    Wicks, F.D.2    Gholson, R.K.3
  • 2
    • 0000344736 scopus 로고
    • Biosynthetic and salvage pathways of pyridine nucleotide coenzymes
    • Everse, J., Anderson, B. M. & You, K.-S., eds Academic Press, USA
    • White, H. B. III (1982) Biosynthetic and salvage pathways of pyridine nucleotide coenzymes, in The pyridine nucleotide coenzymes (Everse, J., Anderson, B. M. & You, K.-S., eds) pp. 225-248, Academic Press, USA.
    • (1982) The Pyridine Nucleotide Coenzymes , pp. 225-248
    • White III, H.B.1
  • 3
    • 0018851537 scopus 로고
    • Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems
    • Foster, J. W. & Moat, A. G. (1980) Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems. Microbiol. Rev. 44, 83-105.
    • (1980) Microbiol. Rev. , vol.44 , pp. 83-105
    • Foster, J.W.1    Moat, A.G.2
  • 4
    • 0025364212 scopus 로고
    • Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase
    • Seifert, J., Kunz, N., Flachmann, R., Laufer, A., Jany, K. D. & Gassen, H. G. (1990) Expression of the E. coli nadB gene and characterization of the gene product L-aspartate oxidase, Biol. Chem. Hoppe-Seyler 371, 239-248.
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , pp. 239-248
    • Seifert, J.1    Kunz, N.2    Flachmann, R.3    Laufer, A.4    Jany, K.D.5    Gassen, H.G.6
  • 6
    • 0017817482 scopus 로고
    • Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins
    • Massey, V. & Hemmerich, P. (1978) Photoreduction of flavoproteins and other biological compounds catalyzed by deazaflavins, Biochemistry 17, 9-17.
    • (1978) Biochemistry , vol.17 , pp. 9-17
    • Massey, V.1    Hemmerich, P.2
  • 7
    • 0028300515 scopus 로고
    • Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from E. coli by alteration of a nearby charged residue, K53R
    • Maeda-Yorita, K., Russel, G. C., Guest, J. R., Massey, V. & Williams, C. H. Jr (1994) Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from E. coli by alteration of a nearby charged residue, K53R, Biochemistry 33, 6213-6220.
    • (1994) Biochemistry , vol.33 , pp. 6213-6220
    • Maeda-Yorita, K.1    Russel, G.C.2    Guest, J.R.3    Massey, V.4    Williams Jr., C.H.5
  • 8
    • 0002435359 scopus 로고
    • A simple method for the determination of redox potentials
    • Curti, B., Ronchi, R. & Zanetti, G., eds Walter de Gruyter & Co., Berlin
    • Massey, V. (1990) A simple method for the determination of redox potentials, in Flavins and flavoproteins (Curti, B., Ronchi, R. & Zanetti, G., eds) pp. 59-66, Walter de Gruyter & Co., Berlin.
    • (1990) Flavins and Flavoproteins , pp. 59-66
    • Massey, V.1
  • 9
    • 0027305020 scopus 로고
    • Synthesis of a fluorescent derivatizing reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography
    • Cohen, S. A. & Michaud, D. P. (1993) Synthesis of a fluorescent derivatizing reagent, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate, and its application for the analysis of hydrolysate amino acids via high-performance liquid chromatography, Anal. Biochem. 211, 279-287.
    • (1993) Anal. Biochem. , vol.211 , pp. 279-287
    • Cohen, S.A.1    Michaud, D.P.2
  • 10
    • 33746190548 scopus 로고
    • A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons
    • Benesi, H. A. & Hildebrand, J. H. (1949) A spectrophotometric investigation of the interaction of iodine with aromatic hydrocarbons, J. Am. Chem. Soc. 71, 2703-2707.
    • (1949) J. Am. Chem. Soc. , vol.71 , pp. 2703-2707
    • Benesi, H.A.1    Hildebrand, J.H.2
  • 11
    • 0021766207 scopus 로고
    • Interaction of the membrane-bound succinate dehydrogenase with substrate and competitive inhibitors
    • Kotlyar, A. B. & Vinogradov, A. D. (1984) Interaction of the membrane-bound succinate dehydrogenase with substrate and competitive inhibitors, Biochim. Biophys. Acta 784, 24-34.
    • (1984) Biochim. Biophys. Acta , vol.784 , pp. 24-34
    • Kotlyar, A.B.1    Vinogradov, A.D.2
  • 12
    • 0015608091 scopus 로고
    • Equilibrium binding of nicotinamide nucleotides to lactate dehydrogenases
    • Stinson, R. A. & Holbrook, J. J. (1973) Equilibrium binding of nicotinamide nucleotides to lactate dehydrogenases, Biochem. J. 131, 719-728.
    • (1973) Biochem. J. , vol.131 , pp. 719-728
    • Stinson, R.A.1    Holbrook, J.J.2
  • 14
    • 0001005014 scopus 로고
    • Structure and function of succinate dehydrogenase and fumarate reductase
    • Muller, F., ed. CRC Press, Boca Raton, FL
    • Ackrell, B. A. C., Johnson, M. K., Gunsalus, R. P. & Cecchini, G. (1991) Structure and function of succinate dehydrogenase and fumarate reductase, in Chemistry and biochemistry of flavoenzymes (Muller, F., ed.) pp. 229-297, CRC Press, Boca Raton, FL.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , pp. 229-297
    • Ackrell, B.A.C.1    Johnson, M.K.2    Gunsalus, R.P.3    Cecchini, G.4
  • 15
    • 0003518480 scopus 로고
    • J. Wiley & Sons, New York
    • Segel, I. H. (1975) Enzyme kinetics, pp. 829-830, J. Wiley & Sons, New York.
    • (1975) Enzyme Kinetics , pp. 829-830
    • Segel, I.H.1
  • 16
    • 0003518480 scopus 로고
    • J. Wiley & Sons, New York
    • Segel, I. H. (1975) Enzyme kinetics, pp. 564-565, J. Wiley & Sons, New York.
    • (1975) Enzyme Kinetics , pp. 564-565
    • Segel, I.H.1
  • 17
    • 0000092520 scopus 로고
    • Purification and properties of fumarate reductase from baker's yeast
    • Muratsubaki, H. & Katsume, T. (1982) Purification and properties of fumarate reductase from baker's yeast, Agric. Biol. Chem. 46, 2909-2917.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 2909-2917
    • Muratsubaki, H.1    Katsume, T.2
  • 18
    • 0021144978 scopus 로고
    • The respiratory chains of Escherichia coli
    • Ingledew, W. J. & Poole, R. K. (1984) The respiratory chains of Escherichia coli, Microbiol. Rev. 48, 222-271.
    • (1984) Microbiol. Rev. , vol.48 , pp. 222-271
    • Ingledew, W.J.1    Poole, R.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.