메뉴 건너뛰기




Volumn 144, Issue 4, 1998, Pages 1113-1121

Fructose and mannose metabolism in Aeromonas hydrophila: Identification of transport systems and catabolic pathways

Author keywords

Aeromonas hydrophila; Catabolic pathways; Fructose; Mannose; Phosphotransferase system

Indexed keywords

FRUCTOSE; FRUCTOSE 1 PHOSPHATE; FRUCTOSE 1,6 BISPHOSPHATE; MANNOSE; PHOSPHOENOLPYRUVATE; PHOSPHOTRANSFERASE;

EID: 0031978751     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-144-4-1113     Document Type: Article
Times cited : (12)

References (50)
  • 1
    • 0016826477 scopus 로고
    • Catabolism of D-fructose and D-ribose by Pseudomonas doudoroffii. I. Physiological studies and mutant analysis
    • Baumann, P. & Baumann, L. (1975). Catabolism of D-fructose and D-ribose by Pseudomonas doudoroffii. I. Physiological studies and mutant analysis. Arch Microbiol 105, 225-240.
    • (1975) Arch Microbiol , vol.105 , pp. 225-240
    • Baumann, P.1    Baumann, L.2
  • 2
    • 0030463224 scopus 로고    scopus 로고
    • Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the glucose and N-acetylglucosamine permeases
    • Bouma, C. L. & Roseman, S. (1996a). Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the glucose and N-acetylglucosamine permeases. J Biol Chem 271, 33457-33467.
    • (1996) J Biol Chem , vol.271 , pp. 33457-33467
    • Bouma, C.L.1    Roseman, S.2
  • 3
    • 0030466994 scopus 로고    scopus 로고
    • Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the mannose/glucose permease
    • Bouma, C. L. & Roseman, S. (1996b). Sugar transport by the marine chitinolytic bacterium Vibrio furnissii. Molecular cloning and analysis of the mannose/glucose permease. J Biol Chem 271, 33468-33475.
    • (1996) J Biol Chem , vol.271 , pp. 33468-33475
    • Bouma, C.L.1    Roseman, S.2
  • 4
    • 0026560830 scopus 로고
    • Man, a component of the phosphoenolpyruvate: Mannose phosphotransferase system
    • Man, a component of the phosphoenolpyruvate: mannose phosphotransferase system. J Gen Microbiol 138, 769-777.
    • (1992) J Gen Microbiol , vol.138 , pp. 769-777
    • Bourassa, S.1    Vadeboncoeur, C.2
  • 5
    • 45949120384 scopus 로고
    • Diversity of the phosphoenolpyruvate: Glucose phosphotransferase system in the Enterobacteriaceae
    • Bouvet, O. M. M. & Grimont, P. A. D. (1987). Diversity of the phosphoenolpyruvate: glucose phosphotransferase system in the Enterobacteriaceae. Ann Inst Pasteur Microbiol 138, 3-13.
    • (1987) Ann Inst Pasteur Microbiol , vol.138 , pp. 3-13
    • Bouvet, O.M.M.1    Grimont, P.A.D.2
  • 6
    • 0028268929 scopus 로고
    • Phenotypic diversity of anaerobic glycerol dissimilation shown by seven enterobacterial species
    • Bouvet, O. M. M., Lenormand, P., Carlier, J. P. & Grimont, P. A. D. (1994). Phenotypic diversity of anaerobic glycerol dissimilation shown by seven enterobacterial species. Res Microbiol 145, 129-139.
    • (1994) Res Microbiol , vol.145 , pp. 129-139
    • Bouvet, O.M.M.1    Lenormand, P.2    Carlier, J.P.3    Grimont, P.A.D.4
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0020570242 scopus 로고
    • Regulation of phosphoenolpyruvate-dependent phosphotransferase system and β-D-phosphogalactoside galactohydrolase activities in Lactobacillus casei
    • Chassy, B. M. & Thompson, J. (1983). Regulation of phosphoenolpyruvate-dependent phosphotransferase system and β-D-phosphogalactoside galactohydrolase activities in Lactobacillus casei. J Bacteriol 154, 1195-1203.
    • (1983) J Bacteriol , vol.154 , pp. 1195-1203
    • Chassy, B.M.1    Thompson, J.2
  • 9
    • 0022515687 scopus 로고
    • Proposal to recognize the family Aeromonadaceae fam. nov.
    • Colwell, R. R., MacDonell, M. T. & DeLey, J. (1986). Proposal to recognize the family Aeromonadaceae fam. nov. Int J Syst Bacteriol 36, 473-477.
    • (1986) Int J Syst Bacteriol , vol.36 , pp. 473-477
    • Colwell, R.R.1    MacDonell, M.T.2    DeLey, J.3
  • 10
    • 0017618227 scopus 로고
    • Different degradation pathways for glucose and fructose in Rhodopseudomonas capsulata
    • Conrad, R. & Schlegel, H. G. (1977). Different degradation pathways for glucose and fructose in Rhodopseudomonas capsulata. Arch Microbiol 112, 39-48.
    • (1977) Arch Microbiol , vol.112 , pp. 39-48
    • Conrad, R.1    Schlegel, H.G.2
  • 11
    • 0024989681 scopus 로고
    • Characterization of Escherichia coli adenylate cyclase mutants with modified regulation
    • Crasnier, M. & Danchin, A. (1990). Characterization of Escherichia coli adenylate cyclase mutants with modified regulation. J Gen Microbiol 136, 1825-1831.
    • (1990) J Gen Microbiol , vol.136 , pp. 1825-1831
    • Crasnier, M.1    Danchin, A.2
  • 12
    • 0016761881 scopus 로고
    • Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase and glucokinase
    • Curtis, S. J. & Epstein, W. (1975). Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase and glucokinase. J Bacteriol 122, 1189-1199.
    • (1975) J Bacteriol , vol.122 , pp. 1189-1199
    • Curtis, S.J.1    Epstein, W.2
  • 13
    • 0026047506 scopus 로고
    • Fructose catabolism in Xanthomonas campestris pv. campestris
    • De Crécy-Lagard, V., Bouvet, O. M. M., Lejeune, P. & Danchin, A. (1991a). Fructose catabolism in Xanthomonas campestris pv. campestris. J Biol Chem 266, 18154-18161.
    • (1991) J Biol Chem , vol.266 , pp. 18154-18161
    • De Crécy-Lagard, V.1    Bouvet, O.M.M.2    Lejeune, P.3    Danchin, A.4
  • 14
    • 0025873598 scopus 로고
    • Identification of two fructose transport and phosphorylation pathways in Xanthomonas campestris pv. campestris
    • De Crécy-Lagard, V., Bouvet, O. M. M., Lejeune, P. & Danchin, A. (1991b). Identification of two fructose transport and phosphorylation pathways in Xanthomonas campestris pv. campestris. Mol Gen Genet 227, 465-472.
    • (1991) Mol Gen Genet , vol.227 , pp. 465-472
    • De Crécy-Lagard, V.1    Bouvet, O.M.M.2    Lejeune, P.3    Danchin, A.4
  • 15
    • 0028840398 scopus 로고
    • Fructose phosphotransferase system of Xanthomonas campestris pv. campestris: Characterization of the fruB gene
    • De Crécy-Lagard, V., Binet, M. & Danchin, A. (1995). Fructose phosphotransferase system of Xanthomonas campestris pv. campestris: characterization of the fruB gene. Microbiology 141, 2253-2260.
    • (1995) Microbiology , vol.141 , pp. 2253-2260
    • De Crécy-Lagard, V.1    Binet, M.2    Danchin, A.3
  • 16
    • 0020065258 scopus 로고
    • Fractionation and characterization of the phosphoenolpyruvate: Fructose 1-phosphotransferase system from Pseudomonas aeruginosa
    • Durham, D. R. & Phibbs, P. V. J. (1982). Fractionation and characterization of the phosphoenolpyruvate: fructose 1-phosphotransferase system from Pseudomonas aeruginosa. J Bacteriol 149, 534-541.
    • (1982) J Bacteriol , vol.149 , pp. 534-541
    • Durham, D.R.1    Phibbs, P.V.J.2
  • 17
    • 0022400657 scopus 로고
    • Man complex of Escherichia coli
    • Man complex of Escherichia coli. J Biol Chem 260, 15495-15503.
    • (1985) J Biol Chem , vol.260 , pp. 15495-15503
    • Erni, B.1    Zanolari, B.2
  • 18
    • 0001199114 scopus 로고
    • The family Vibrionaceae
    • Edited by A. Balows, H. G. Trüper, M. Dworkin, W. Harder & K.-H. Schleifer. New York: Springer
    • Farmer, J. J., III (1992). The family Vibrionaceae. In The Prokaryotes, 2nd edn, pp. 2938-2951. Edited by A. Balows, H. G. Trüper, M. Dworkin, W. Harder & K.-H. Schleifer. New York: Springer.
    • (1992) The Prokaryotes, 2nd Edn , pp. 2938-2951
    • Farmer III, J.J.1
  • 19
    • 0001156459 scopus 로고
    • The genera Aeromonas and Plesiomonas
    • Edited by A. Balows, H. G. Trüper, M. Dworkin, W. Harder & K.-H. Schleifer. New York: Springer
    • Farmer, J. J., III, Arduino, M. J. & Hickman-Brenner, F. W. (1992). The genera Aeromonas and Plesiomonas. In The Prokaryotes, 2nd edn, pp. 3013-3045. Edited by A. Balows, H. G. Trüper, M. Dworkin, W. Harder & K.-H. Schleifer. New York: Springer.
    • (1992) The Prokaryotes, 2nd Edn , pp. 3013-3045
    • Farmer III, J.J.1    Arduino, M.J.2    Hickman-Brenner, F.W.3
  • 20
    • 0015581911 scopus 로고
    • The utilization of fructose by Escherichia coli
    • Ferenci, T. & Kornberg, H. L. (1973). The utilization of fructose by Escherichia coli. Biochem J 132, 341-347.
    • (1973) Biochem J , vol.132 , pp. 341-347
    • Ferenci, T.1    Kornberg, H.L.2
  • 21
    • 0016269294 scopus 로고
    • Role of PTS mediated synthesis of fructose-1-P and fructose-6-P in the growth of Escherichia coli on fructose
    • Ferenci, T. & Kornberg, H. L. (1974). Role of PTS mediated synthesis of fructose-1-P and fructose-6-P in the growth of Escherichia coli on fructose. Proc R Soc Lond Ser B 187, 105-119.
    • (1974) Proc R Soc Lond Ser B , vol.187 , pp. 105-119
    • Ferenci, T.1    Kornberg, H.L.2
  • 22
    • 0018818715 scopus 로고
    • Fine control of adenylate cyclase by the phosphoenolpyruvate sugar phosphotransferase systems in Escherichia coli and Salmonella typhimurium
    • Feucht, B. U. & Saier, M. H., Jr (1980). Fine control of adenylate cyclase by the phosphoenolpyruvate sugar phosphotransferase systems in Escherichia coli and Salmonella typhimurium. J Bacteriol 141, 603-610.
    • (1980) J Bacteriol , vol.141 , pp. 603-610
    • Feucht, B.U.1    Saier Jr., M.H.2
  • 24
    • 0014327572 scopus 로고
    • Phosphoenolpyruvate-dependent formation of D-fructose-1-phosphate by a four-component phosphotransferase system
    • Hanson, T. E. & Anderson, R. L. (1968). Phosphoenolpyruvate-dependent formation of D-fructose-1-phosphate by a four-component phosphotransferase system. Proc Natl Acad Sci USA 61, 269-276.
    • (1968) Proc Natl Acad Sci USA , vol.61 , pp. 269-276
    • Hanson, T.E.1    Anderson, R.L.2
  • 25
    • 84981803223 scopus 로고
    • Polysaccharide B-1459: A new hydrocolloid polyelectrolyte produced from glucose by bacterial fermentation
    • Jeanes, A., Pittsley, J. E. & Senti, F. R. (1961). Polysaccharide B-1459: a new hydrocolloid polyelectrolyte produced from glucose by bacterial fermentation. J Appl Polym Sci 5, 519-526.
    • (1961) J Appl Polym Sci , vol.5 , pp. 519-526
    • Jeanes, A.1    Pittsley, J.E.2    Senti, F.R.3
  • 26
    • 0016290249 scopus 로고
    • Genetic analysis of fructose utilization by Escherichia coli
    • Jones-Mortimer, M. C. & Kornberg, H. L. (1974). Genetic analysis of fructose utilization by Escherichia coli. Proc R Soc Lond Ser B 187, 121-131.
    • (1974) Proc R Soc Lond Ser B , vol.187 , pp. 121-131
    • Jones-Mortimer, M.C.1    Kornberg, H.L.2
  • 27
    • 0018424661 scopus 로고
    • Separation of four components of the phosphoenolpyruvate:glucose phosphotransferase system in Vibrio parahaemolyticus
    • Kubota, Y., Iuchi, S., Fujisawa, A. & Tanaka, S. (1979). Separation of four components of the phosphoenolpyruvate:glucose phosphotransferase system in Vibrio parahaemolyticus. Microbiol Immunol 23, 131-146.
    • (1979) Microbiol Immunol , vol.23 , pp. 131-146
    • Kubota, Y.1    Iuchi, S.2    Fujisawa, A.3    Tanaka, S.4
  • 28
    • 0018344758 scopus 로고
    • Influence of the lactose plasmid on the metabolism of galactose by Streptococcus lactis
    • Leblanc, D. J., Crow, V. L., Lee, L. N. & Garon, C. F. (1979). Influence of the lactose plasmid on the metabolism of galactose by Streptococcus lactis. J Bacteriol 137, 878-884.
    • (1979) J Bacteriol , vol.137 , pp. 878-884
    • Leblanc, D.J.1    Crow, V.L.2    Lee, L.N.3    Garon, C.F.4
  • 29
    • 0014072244 scopus 로고
    • Adenosine triphosphate-linked control of Pseudomonas aeruginosa glucose-6-phosphate dehydrogenase
    • Lessie, T. G. & Neidhart, F. C. (1967). Adenosine triphosphate-linked control of Pseudomonas aeruginosa glucose-6-phosphate dehydrogenase. J Bacteriol 93, 1337-1345.
    • (1967) J Bacteriol , vol.93 , pp. 1337-1345
    • Lessie, T.G.1    Neidhart, F.C.2
  • 30
    • 0025022359 scopus 로고
    • Cyclic AMP synthesis in Escherichia coli strains bearing known deletions in the pts phosphotransferase operon
    • Lévy, S., Zeng, G. Q. & Danchin, A. (1990). Cyclic AMP synthesis in Escherichia coli strains bearing known deletions in the pts phosphotransferase operon. Gene 86, 27-33.
    • (1990) Gene , vol.86 , pp. 27-33
    • Lévy, S.1    Zeng, G.Q.2    Danchin, A.3
  • 33
    • 0023442377 scopus 로고
    • Phosphoenolpyruvate:glucose phosphotransferase system in species of Vibrio, a widely distributed marine bacterial genus
    • Meadow, N. D., Revuelta, R., Chen, V. N., Colwell, R. R. & Roseman, S. (1987). Phosphoenolpyruvate:glucose phosphotransferase system in species of Vibrio, a widely distributed marine bacterial genus. J Bacteriol 169, 4893-4900.
    • (1987) J Bacteriol , vol.169 , pp. 4893-4900
    • Meadow, N.D.1    Revuelta, R.2    Chen, V.N.3    Colwell, R.R.4    Roseman, S.5
  • 34
  • 35
    • 0021858740 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase system of bacteria
    • Postma, P. W. & Lengeler, J. W. (1985). Phosphoenolpyruvate: carbohydrate phosphotransferase system of bacteria. Microbiol Rev 49, 232-269.
    • (1985) Microbiol Rev , vol.49 , pp. 232-269
    • Postma, P.W.1    Lengeler, J.W.2
  • 36
    • 0018901629 scopus 로고
    • Enzymes II of the phosphotransferase system do not catalyse sugar transport in the absence of phosphorylation
    • Postma, P. W. & Stock, J. B. (1980). Enzymes II of the phosphotransferase system do not catalyse sugar transport in the absence of phosphorylation. J Bacteriol 141, 476-484.
    • (1980) J Bacteriol , vol.141 , pp. 476-484
    • Postma, P.W.1    Stock, J.B.2
  • 37
    • 0027291428 scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase systems of bacteria
    • Postma, P. W., Lengeler, J. W. & Jacobson, G. R. (1993). Phosphoenolpyruvate: carbohydrate phosphotransferase systems of bacteria. Microbiol Rev 57, 543-594.
    • (1993) Microbiol Rev , vol.57 , pp. 543-594
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 38
    • 0019159696 scopus 로고
    • Substrate specificity and kinetic characterization of sugar uptake and phosphorylation, catalyzed by the mannose enzyme II of the phosphotransferase system in Salmonella typhimurium
    • Rephaeli, A. W. & Saier, M. H., Jr (1980). Substrate specificity and kinetic characterization of sugar uptake and phosphorylation, catalyzed by the mannose enzyme II of the phosphotransferase system in Salmonella typhimurium. J Biol Chem 255, 8585-8591.
    • (1980) J Biol Chem , vol.255 , pp. 8585-8591
    • Rephaeli, A.W.1    Saier Jr., M.H.2
  • 39
    • 0015240501 scopus 로고
    • Phosphoenolpyruvate-dependent fructose phosphorylation in photosynthetic bacteria
    • Saier, M. H., Jr, Feucht, B. U. & Roseman, S. (1971). Phosphoenolpyruvate-dependent fructose phosphorylation in photosynthetic bacteria. J Biol Chem 246, 7819-7821.
    • (1971) J Biol Chem , vol.246 , pp. 7819-7821
    • Saier Jr., M.H.1    Feucht, B.U.2    Roseman, S.3
  • 40
    • 0017139277 scopus 로고
    • Sugar transport. Properties of mutant bacteria defective in proteins of the phosphoenolpyruvate: Sugar phosphotransferase system
    • Saier, M. H., Jr, Simoni, R. D. & Roseman, S. (1976). Sugar transport. Properties of mutant bacteria defective in proteins of the phosphoenolpyruvate: sugar phosphotransferase system. J Biol Chem 251, 6584-6597.
    • (1976) J Biol Chem , vol.251 , pp. 6584-6597
    • Saier Jr., M.H.1    Simoni, R.D.2    Roseman, S.3
  • 41
    • 0019497160 scopus 로고
    • Competition between two pathways for sugar uptake by the phosphoenolpyruvate-dependent sugar phosphotransferase system in Salmonella typhimurium
    • Scholte, B. J. & Postma, P. W. (1981). Competition between two pathways for sugar uptake by the phosphoenolpyruvate-dependent sugar phosphotransferase system in Salmonella typhimurium. Eur J Biochem 114, 51-58.
    • (1981) Eur J Biochem , vol.114 , pp. 51-58
    • Scholte, B.J.1    Postma, P.W.2
  • 43
    • 0014055981 scopus 로고
    • Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol
    • Tanaka, S., Lerner, S. A. & Lin, E. (1967). Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol. J Bacteriol 93, 642-648.
    • (1967) J Bacteriol , vol.93 , pp. 642-648
    • Tanaka, S.1    Lerner, S.A.2    Lin, E.3
  • 44
    • 0030901004 scopus 로고    scopus 로고
    • Virulence properties of clinically significant Aeromonas species: Evidence for pathogenicity
    • Thornley, J. P., Shaw, J. G., Gryllos, I. A. & Eley, A. (1997). Virulence properties of clinically significant Aeromonas species: evidence for pathogenicity. Rev Med Microbiol 8, 61-72.
    • (1997) Rev Med Microbiol , vol.8 , pp. 61-72
    • Thornley, J.P.1    Shaw, J.G.2    Gryllos, I.A.3    Eley, A.4
  • 45
    • 0029802868 scopus 로고    scopus 로고
    • Comparative analysis of the cya locus in enterobacteria and related Gram-negative facultative anaerobes
    • Trotot, P., Sismeiro, O., Vivarès, C., Glaser, P., Bresson-Roy, A. & Danchin, A. (1996). Comparative analysis of the cya locus in enterobacteria and related Gram-negative facultative anaerobes. Biochimie 78, 277-287.
    • (1996) Biochimie , vol.78 , pp. 277-287
    • Trotot, P.1    Sismeiro, O.2    Vivarès, C.3    Glaser, P.4    Bresson-Roy, A.5    Danchin, A.6
  • 46
    • 0343688255 scopus 로고
    • A two dimensional system of paper chromatography of some sugar phosphates
    • Wawszkiewicz, E. J. (1961). A two dimensional system of paper chromatography of some sugar phosphates. Anal Chem 33, 252-254.
    • (1961) Anal Chem , vol.33 , pp. 252-254
    • Wawszkiewicz, E.J.1
  • 48
    • 0022859359 scopus 로고
    • Pel, the protein that permits γ DNA penetration of E. coli, is encoded by a gene in pts M and is required for mannose utilization by the phosphotransferase system
    • Williams, N. D., Fox, K., Shea, C. & Roseman, S. (1986). Pel, the protein that permits γ DNA penetration of E. coli, is encoded by a gene in pts M and is required for mannose utilization by the phosphotransferase system. Proc Natl Acad Sci USA 83, 8934-8938.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8934-8938
    • Williams, N.D.1    Fox, K.2    Shea, C.3    Roseman, S.4
  • 49
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese, C. R. (1987). Bacterial evolution. Microbiol Rev 51, 221-271.
    • (1987) Microbiol Rev , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 50
    • 0025340681 scopus 로고
    • Structure and evolution of a multidomain multiphosphoryl transfer protein. Nucleotide sequence of the fruB (HI) gene in Rhodobacter capsulatus and comparisons with homologous genes from other organisms
    • Wu, L. F., Tomich, J. M. & Saier, M. H., Jr (1990). Structure and evolution of a multidomain multiphosphoryl transfer protein. Nucleotide sequence of the fruB (HI) gene in Rhodobacter capsulatus and comparisons with homologous genes from other organisms. J Mol Biol 213, 687-703.
    • (1990) J Mol Biol , vol.213 , pp. 687-703
    • Wu, L.F.1    Tomich, J.M.2    Saier Jr., M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.