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Volumn 58, Issue 2-4, 1997, Pages 261-276

Characterization of H. parasuis periplasmic nucleotide pyrophosphatase as a potential target enzyme for inhibition of growth

Author keywords

Growth inhibition; Haemophilus parasuis; Nucleotide pyrophosphatase; Pyridine nucleotide analogs

Indexed keywords

3 AMINOPYRIDINE MONONUCLEOTIDE; ADENOSINE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ANTIINFECTIVE AGENT; CYTIDINE DIPHOSPHATE; ENZYME INHIBITOR; GUANOSINE DIPHOSPHATE; NICOTINAMIDE DERIVATIVE; NICOTINAMIDE NUCLEOTIDE; NUCLEOTIDE PYROPHOSPHATASE; PYRIDINE NUCLEOTIDE; PYRIMIDINE NUCLEOTIDE; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE;

EID: 0031470731     PISSN: 03781135     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1135(97)00149-1     Document Type: Article
Times cited : (2)

References (44)
  • 1
    • 0013773989 scopus 로고
    • A hydrophobic region at the active site of yeast alcohol dehydrogenase
    • Anderson, B.M., Anderson, C.D., 1964. A hydrophobic region at the active site of yeast alcohol dehydrogenase. Biochim. Biophys. Res. Commun. 16 (3), 258-262.
    • (1964) Biochim. Biophys. Res. Commun. , vol.16 , Issue.3 , pp. 258-262
    • Anderson, B.M.1    Anderson, C.D.2
  • 2
    • 0013970390 scopus 로고
    • Nicotinamide adenine dinucleotide pyrophosphatase in the growing and aging mosquito
    • Anderson, B.M., Lang, C.A., 1966. Nicotinamide adenine dinucleotide pyrophosphatase in the growing and aging mosquito. Biochem. J. 101, 392-396.
    • (1966) Biochem. J. , vol.101 , pp. 392-396
    • Anderson, B.M.1    Lang, C.A.2
  • 3
    • 0014027334 scopus 로고
    • Inhibition of glutamic dehydrogenase by N'-alkylnicotinamide chlorides
    • Anderson, B.M., Reynolds, M.L., 1966. Inhibition of glutamic dehydrogenase by N'-alkylnicotinamide chlorides. J. Biol. Chem. 241 (8), 1688-1693.
    • (1966) J. Biol. Chem. , vol.241 , Issue.8 , pp. 1688-1693
    • Anderson, B.M.1    Reynolds, M.L.2
  • 4
    • 0011128914 scopus 로고
    • Hydrophobic interactions of inhibitors with yeast alcohol dehydrogenase
    • Anderson, B.M., Reynolds, M.L., Anderson, C.D., 1965. Hydrophobic interactions of inhibitors with yeast alcohol dehydrogenase. Biochim. Biophys. Acta 99, 46-55.
    • (1965) Biochim. Biophys. Acta , vol.99 , pp. 46-55
    • Anderson, B.M.1    Reynolds, M.L.2    Anderson, C.D.3
  • 5
    • 0022559118 scopus 로고
    • Snake venom NAD glycohydrolase, purification, immobilization, and transglycosidation
    • Anderson, B.M., Yost, D.A., Anderson, C.D., 1986. Snake venom NAD glycohydrolase, purification, immobilization, and transglycosidation. Meth. Enzymol. 122, 173-181.
    • (1986) Meth. Enzymol. , vol.122 , pp. 173-181
    • Anderson, B.M.1    Yost, D.A.2    Anderson, C.D.3
  • 6
    • 0016788478 scopus 로고
    • Pigeon liver NAD kinase. The structural and kinetic basis of regulation of NADPH
    • Apps, O.K., 1975. Pigeon liver NAD kinase. The structural and kinetic basis of regulation of NADPH. Eur. J. Biochem. 55, 475-483.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 475-483
    • Apps, O.K.1
  • 8
    • 0019332921 scopus 로고
    • The nature of negative cooperativity in alkaline phosphatase. Kinetic patterns contrary to the flip-flop model
    • Bale, J.R., Chock, P.B., Huang, C.Y., 1980. The nature of negative cooperativity in alkaline phosphatase. Kinetic patterns contrary to the flip-flop model. J. Biol. Chem. 255, 8424-8430.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8424-8430
    • Bale, J.R.1    Chock, P.B.2    Huang, C.Y.3
  • 9
    • 0016824465 scopus 로고
    • Interconversion of different molecular weight forms of human erythrocyte orotidylate decarboxylase
    • Brown, G.K., Fox, R.M., O'Sullivan, W.J., 1975. Interconversion of different molecular weight forms of human erythrocyte orotidylate decarboxylase. J. Biol. Chem. 250, 7352-7358.
    • (1975) J. Biol. Chem. , vol.250 , pp. 7352-7358
    • Brown, G.K.1    Fox, R.M.2    O'Sullivan, W.J.3
  • 10
    • 0019278741 scopus 로고
    • Studies of bovine seminal fluid nucleotide pyrophosphatase
    • Buckon, M.E., Anderson, B.M., 1980. Studies of bovine seminal fluid nucleotide pyrophosphatase. Arch. Biochem. Biophys. 202, 396-404.
    • (1980) Arch. Biochem. Biophys. , vol.202 , pp. 396-404
    • Buckon, M.E.1    Anderson, B.M.2
  • 12
    • 0018845618 scopus 로고
    • Preparation and purification of nicotinamide mononucleotide analogs
    • Christ, W., Cooper, H., 1980. Preparation and purification of nicotinamide mononucleotide analogs. Meth. Enzymol. 66, 71-81.
    • (1980) Meth. Enzymol. , vol.66 , pp. 71-81
    • Christ, W.1    Cooper, H.2
  • 13
    • 77956993063 scopus 로고
    • Procedures for the determination of pyridine nucleotides
    • Ciotti, M.M., Kaplan, N.O., 1957. Procedures for the determination of pyridine nucleotides. Meth. Enzymol. 3, 890-892.
    • (1957) Meth. Enzymol. , vol.3 , pp. 890-892
    • Ciotti, M.M.1    Kaplan, N.O.2
  • 15
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W.W., 1979. Statistical analysis of enzyme kinetic data. Meth. Enzymol. 63, 103-138.
    • (1979) Meth. Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 16
    • 0002003092 scopus 로고
    • Helicobacter pylori: A bacterial cause of gastritis, peptic ulcer disease, and gastric cancer
    • Clover, T.L., Blaser, M.J., 1995. Helicobacter pylori: a bacterial cause of gastritis, peptic ulcer disease, and gastric cancer. ASM News 61, 21-26.
    • (1995) ASM News , vol.61 , pp. 21-26
    • Clover, T.L.1    Blaser, M.J.2
  • 17
    • 0000459625 scopus 로고
    • Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase
    • Dalziel, K., Engle, P., 1968. Antagonistic homotropic interactions as a possible explanation of coenzyme activation of glutamate dehydrogenase. FEBS Lett. 1, 349-352.
    • (1968) FEBS Lett. , vol.1 , pp. 349-352
    • Dalziel, K.1    Engle, P.2
  • 18
    • 0018166487 scopus 로고
    • An enzyme degrading reduced nicotinamide adenine dinucleotide in Proteus vulgaris
    • Davies, R., King, H.K., 1978. An enzyme degrading reduced nicotinamide adenine dinucleotide in Proteus vulgaris. Biochem. J. 175, 669-674.
    • (1978) Biochem. J. , vol.175 , pp. 669-674
    • Davies, R.1    King, H.K.2
  • 19
    • 0025273613 scopus 로고
    • Studies of NAD kinase and NMN:ATP adenylyltranferase in Haemophilus influenzae
    • Denicola-Seoane, A., Anderson, B.M., 1990. Studies of NAD kinase and NMN:ATP adenylyltranferase in Haemophilus influenzae. J. Gen. Microbiol. 136, 425-430.
    • (1990) J. Gen. Microbiol. , vol.136 , pp. 425-430
    • Denicola-Seoane, A.1    Anderson, B.M.2
  • 20
    • 0015500555 scopus 로고
    • Purification and properties of a yeast nucleotide pyrophosphatase
    • Haroz, R.K., Twu, J.S., Brethauer, R.K., 1972. Purification and properties of a yeast nucleotide pyrophosphatase. J. Biol. Chem. 247, 1452-1457.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1452-1457
    • Haroz, R.K.1    Twu, J.S.2    Brethauer, R.K.3
  • 24
    • 0023038242 scopus 로고
    • Characterization of Haemophilus influenzae nucleotide pyrophosphatase an enzyme of critical importance for the growth of the organism
    • Kahn, D.W., Anderson, B.M., 1986. Characterization of Haemophilus influenzae nucleotide pyrophosphatase an enzyme of critical importance for the growth of the organism. J. Biol. Chem. 261 (13), 6016-6025.
    • (1986) J. Biol. Chem. , vol.261 , Issue.13 , pp. 6016-6025
    • Kahn, D.W.1    Anderson, B.M.2
  • 25
    • 0017253675 scopus 로고
    • A taxonomic study of the genus Haemophilus, with the proposal of a new species
    • Killian, M., 1976. A taxonomic study of the genus Haemophilus, with the proposal of a new species. J. Gen. Microbiol. 93, 9-62.
    • (1976) J. Gen. Microbiol. , vol.93 , pp. 9-62
    • Killian, M.1
  • 26
    • 0014429802 scopus 로고
    • Properties of nicotinamide adenine dinucleotide-binding sites of L-α-glycerophosphate dehydrogenase
    • Kim, S.J., Anderson, B.M., 1968. Properties of nicotinamide adenine dinucleotide-binding sites of L-α-glycerophosphate dehydrogenase. J. Biol. Chem. 243 (12), 3351-3356.
    • (1968) J. Biol. Chem. , vol.243 , Issue.12 , pp. 3351-3356
    • Kim, S.J.1    Anderson, B.M.2
  • 27
    • 0015322387 scopus 로고
    • Studies on nucleotide pyrophosphatase: I. Partial purification and properties of a sheep liver enzyme that catalyzes the hydrolysis of dinucleotides
    • Krishnan, N., Rao, N.A., 1972. Studies on nucleotide pyrophosphatase: I. Partial purification and properties of a sheep liver enzyme that catalyzes the hydrolysis of dinucleotides. Arch. Biochem. Biophys. 149, 336-348.
    • (1972) Arch. Biochem. Biophys. , vol.149 , pp. 336-348
    • Krishnan, N.1    Rao, N.A.2
  • 28
    • 0013797726 scopus 로고
    • Nucleotidases in plants: I. Partial purification and properties of the enzyme hydrolyzing flavin adenine dinucleotide from mung bean seedlings Phaseolus radiatus
    • Kumar, S.A., Rao, N.A., Vaidyanathan, C.S., 1965. Nucleotidases in plants: I. Partial purification and properties of the enzyme hydrolyzing flavin adenine dinucleotide from mung bean seedlings Phaseolus radiatus. Arch. Biochem. Biophys. 111, 646-652.
    • (1965) Arch. Biochem. Biophys. , vol.111 , pp. 646-652
    • Kumar, S.A.1    Rao, N.A.2    Vaidyanathan, C.S.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of the bacteriophage T4
    • Laemmli, U.K., 1970. Cleavage of structural proteins during assembly of the head of the bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0012452380 scopus 로고
    • Clässer's on the increase
    • Larsen, L.P., 1990. Clässer's on the increase. Pig Int. 20 (22), 24.
    • (1990) Pig Int. , vol.20 , Issue.22 , pp. 24
    • Larsen, L.P.1
  • 31
    • 0016298437 scopus 로고
    • Regulatory behavior of monomeric enzymes: II. A wheat-germ hexokinase a mnemonical enzyme
    • Meunier, J.-C., Buc, J., Navarro, A., Ricard, J., 1974. Regulatory behavior of monomeric enzymes: II. A wheat-germ hexokinase a mnemonical enzyme. Eur. J. Biochem. 49, 209-223.
    • (1974) Eur. J. Biochem. , vol.49 , pp. 209-223
    • Meunier, J.-C.1    Buc, J.2    Navarro, A.3    Ricard, J.4
  • 32
    • 0015921167 scopus 로고
    • Purification and properties of NADP pyrophosphatase from Proteus vulgaris
    • Nakajima, Y., Fukunga, N., Sasaki, S., Usami, S., 1973. Purification and properties of NADP pyrophosphatase from Proteus vulgaris. Biochim. Biophys. Acta 293, 242-255.
    • (1973) Biochim. Biophys. Acta , vol.293 , pp. 242-255
    • Nakajima, Y.1    Fukunga, N.2    Sasaki, S.3    Usami, S.4
  • 33
    • 0016411698 scopus 로고
    • An outbreak of Glässer's disease. Studies on etiology, serology, and effect of vaccination
    • Neilson, R., Danielsen, V., 1975. An outbreak of Glässer's disease. Studies on etiology, serology, and effect of vaccination. Nord. Vet. Med. 27, 20-25.
    • (1975) Nord. Vet. Med. , vol.27 , pp. 20-25
    • Neilson, R.1    Danielsen, V.2
  • 34
    • 0011908451 scopus 로고
    • Haemophilus infections
    • Leman, A.D., Clock, R.D., Mengeling, W.L., Penny, R.H.C., Scholl, E., Straw, B. (Eds.), Iowa State Univ. Press, Ames, IA
    • Nicolet, J., Scholl, E., 1981. Haemophilus infections. In: Leman, A.D., Clock, R.D., Mengeling, W.L., Penny, R.H.C., Scholl, E., Straw, B. (Eds.), Diseases of swine, 5th edn. Iowa State Univ. Press, Ames, IA, pp. 368-377.
    • (1981) Diseases of Swine, 5th Edn. , pp. 368-377
    • Nicolet, J.1    Scholl, E.2
  • 35
    • 0022744328 scopus 로고
    • Tryptone-yeast extract broth as a culture medium for Haemophilus pleuropneumoniae and Haemophilus parasuis to be used as challenge inocula
    • O'Reilly, T., Niven, D.F., 1986a. Tryptone-yeast extract broth as a culture medium for Haemophilus pleuropneumoniae and Haemophilus parasuis to be used as challenge inocula. Can. J. Vet. Res. 50, 441-443.
    • (1986) Can. J. Vet. Res. , vol.50 , pp. 441-443
    • O'Reilly, T.1    Niven, D.F.2
  • 36
    • 0022538012 scopus 로고
    • Defining the metabolic and growth responses of porcine haemophili to exogenous pyridine nucleotides and precursors
    • O'Reilly, T., Niven, D.F., 1986b. Defining the metabolic and growth responses of porcine haemophili to exogenous pyridine nucleotides and precursors. J. Gen. Microbiol. 132, 807-818.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 807-818
    • O'Reilly, T.1    Niven, D.F.2
  • 37
    • 0242476654 scopus 로고
    • The purification and properties of a nucleotide pyrophosphatase of rat liver nuclei
    • Schliselfeld, L.H., Van Eys, J., Touster, O., 1965. The purification and properties of a nucleotide pyrophosphatase of rat liver nuclei. J. Biol. Chem. 240, 811-818.
    • (1965) J. Biol. Chem. , vol.240 , pp. 811-818
    • Schliselfeld, L.H.1    Van Eys, J.2    Touster, O.3
  • 38
    • 0024743347 scopus 로고
    • Preliminary assessment of a Haemophilus parasuis bacterin for use in specific pathogen free swine
    • Smart, N.L., Miniats, O.P., 1989. Preliminary assessment of a Haemophilus parasuis bacterin for use in specific pathogen free swine. Can. J. Vet. Res. 53 (4), 390-393.
    • (1989) Can. J. Vet. Res. , vol.53 , Issue.4 , pp. 390-393
    • Smart, N.L.1    Miniats, O.P.2
  • 39
    • 0024040612 scopus 로고
    • Analysis of Haemophilus parasuis isolates from southern Ontario swine by restriction endonuclease fingerprinting
    • Smart, N.L., Miniats, O.P., MacInnes, J.I., 1988. Analysis of Haemophilus parasuis isolates from southern Ontario swine by restriction endonuclease fingerprinting. Can. J. Vet. Res. 52, 319-324.
    • (1988) Can. J. Vet. Res. , vol.52 , pp. 319-324
    • Smart, N.L.1    Miniats, O.P.2    MacInnes, J.I.3
  • 40
    • 0028212098 scopus 로고
    • Periplasmic location of Brucella abortus Cu/Zn Superoxide dismutase
    • Stabel, T.J., Sha, Z., Mayfield, J.E., 1994. Periplasmic location of Brucella abortus Cu/Zn Superoxide dismutase. Vet. Microbiol. 38, 307-314.
    • (1994) Vet. Microbiol. , vol.38 , pp. 307-314
    • Stabel, T.J.1    Sha, Z.2    Mayfield, J.E.3
  • 41
    • 0008266460 scopus 로고
    • A heat-activated diphosphopyridine nucleotide pyrophosphatase from Proteus vulgaris
    • Swartz, M.N., Kaplan, N.O., Lamborg, M.F., 1958. A heat-activated diphosphopyridine nucleotide pyrophosphatase from Proteus vulgaris. J. Biol. Chem. 232, 1051-1063.
    • (1958) J. Biol. Chem. , vol.232 , pp. 1051-1063
    • Swartz, M.N.1    Kaplan, N.O.2    Lamborg, M.F.3
  • 42
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacryl-amide gel electrophoresis
    • Weber, K., Osborn, M., 1969. The reliability of molecular weight determinations by dodecyl sulfate-polyacryl-amide gel electrophoresis. J. Biol. Chem. 244, 4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 43
    • 0019497607 scopus 로고
    • Purification and properties of the soluble NAD glycohydrolase from Bungarus fasciatus venom
    • Yost, D.A., Andersen, B.M., 1982a. Purification and properties of the soluble NAD glycohydrolase from Bungarus fasciatus venom. J. Biol. Chem. 256, 3647-3653.
    • (1982) J. Biol. Chem. , vol.256 , pp. 3647-3653
    • Yost, D.A.1    Andersen, B.M.2
  • 44
    • 0020490204 scopus 로고
    • Studies of Bungarus fasciatus venom NAD glycohydrolase
    • Yost, D.A., Anderson, B.M., 1982b. Studies of Bungarus fasciatus venom NAD glycohydrolase. J. Biol. Chem. 257, 767-772.
    • (1982) J. Biol. Chem. , vol.257 , pp. 767-772
    • Yost, D.A.1    Anderson, B.M.2


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