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Volumn 187, Issue 24, 2005, Pages 8322-8331

The maltodextrin system of Escherichia coli: Metabolism and transport

Author keywords

[No Author keywords available]

Indexed keywords

CARBON 14; GLYCOGEN; MALTODEXTRIN; MALTOSE;

EID: 28844506194     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.24.8322-8331.2005     Document Type: Article
Times cited : (88)

References (66)
  • 1
    • 0019120076 scopus 로고
    • Identification of a cytoplasmic membrane-associated component of the maltose transport system of Escherichia coli
    • Bavoil, P., M. Hofnung, and H. Nikaido. 1980. Identification of a cytoplasmic membrane-associated component of the maltose transport system of Escherichia coli. J. Biol. Chem. 255:8366-8369.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8366-8369
    • Bavoil, P.1    Hofnung, M.2    Nikaido, H.3
  • 2
    • 0036479107 scopus 로고    scopus 로고
    • Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli. Implications for mal gene regulation, inducer exclusion, and subunit assembly
    • Böhm, A., J. Diez, K. Diederichs, W. Welte, and W. Boos. 2002. Structural model of MalK, the ABC subunit of the maltose transporter of Escherichia coli. Implications for mal gene regulation, inducer exclusion, and subunit assembly. J. Biol. Chem. 277:3708-3717.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3708-3717
    • Böhm, A.1    Diez, J.2    Diederichs, K.3    Welte, W.4    Boos, W.5
  • 3
    • 0019443117 scopus 로고
    • Formation and excretion of acetylmaltose after accumulation of maltose in Escherichia coli
    • Boos, W., T. Ferenci, and H. A. Shuman. 1981. Formation and excretion of acetylmaltose after accumulation of maltose in Escherichia coli. J. Bacteriol. 146:725-732.
    • (1981) J. Bacteriol. , vol.146 , pp. 725-732
    • Boos, W.1    Ferenci, T.2    Shuman, H.A.3
  • 4
    • 0001769249 scopus 로고    scopus 로고
    • Periplasmic binding protein-dependent ABC transporters
    • F. C. Neidhardt, R. Curtiss, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). American Society for Microbiology, Washington, D.C.
    • Boos, W., and J. M. Lucht. 1996. Periplasmic binding protein-dependent ABC transporters, p. 1175-1209. In F. C. Neidhardt, R. Curtiss, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, 2nd ed., vol. 1. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 1175-1209
    • Boos, W.1    Lucht, J.M.2
  • 5
    • 0031887807 scopus 로고    scopus 로고
    • The maltose/maltodextrin system of Escherichia coli: Transport, metabolism, and regulation
    • Boos, W., and H. A. Shuman. 1998. The maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation. Microbiol. Mol. Biol. Rev. 62:204-229.
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 204-229
    • Boos, W.1    Shuman, H.A.2
  • 6
    • 0034283843 scopus 로고    scopus 로고
    • Learning new tricks from an old dog. MalT of the Escherichia coli maltose system is part of a complex regulatory network
    • Boos, W., and A. Böhm. 2000. Learning new tricks from an old dog. MalT of the Escherichia coli maltose system is part of a complex regulatory network. Trends Genet. 16:404-409.
    • (2000) Trends Genet. , vol.16 , pp. 404-409
    • Boos, W.1    Böhm, A.2
  • 8
    • 0025900058 scopus 로고
    • Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20.000
    • Brand, B., and W. Boos. 1991. Maltose transacetylase of Escherichia coli. Mapping and cloning of its structural gene, mac, and characterization of the enzyme as a dimer of identical polypeptides with a molecular weight of 20.000. J. Biol. Chem. 266:14113-14118.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14113-14118
    • Brand, B.1    Boos, W.2
  • 9
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
    • Casadaban, M. J. 1976. Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J. Mol. Biol. 104:541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 10
    • 0020338594 scopus 로고
    • Expression of malT, the regulator gene of the maltose region in Escherichia coli, is limited both at transcription and translation
    • Chapon, C. 1982. Expression of malT, the regulator gene of the maltose region in Escherichia coli, is limited both at transcription and translation. EMBO J. 1:369-374.
    • (1982) EMBO J. , vol.1 , pp. 369-374
    • Chapon, C.1
  • 11
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen, J., G. Lu, J. Lin, A. L. Davidson, and F. A. Quiocho. 2003. A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12:651-661.
    • (2003) Mol. Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davidson, A.L.4    Quiocho, F.A.5
  • 12
    • 0035852667 scopus 로고    scopus 로고
    • Trapping the transition state of an ATP-binding cassette transporter: Evidence for a concerted mechanism of maltose transport
    • Chen, J., S. Sharma, F. A. Quiocho, and A. L. Davidson. 2001. Trapping the transition state of an ATP-binding cassette transporter: evidence for a concerted mechanism of maltose transport. Proc. Natl. Acad. Sci. USA 98:1525-1530.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1525-1530
    • Chen, J.1    Sharma, S.2    Quiocho, F.A.3    Davidson, A.L.4
  • 13
    • 0025353955 scopus 로고
    • Cellular localization of the MalG protein from the maltose transport system in Escherichia coli K12
    • Dassa, E. 1990. Cellular localization of the MalG protein from the maltose transport system in Escherichia coli K12. Mol. Gen. Genet. 222:33-36.
    • (1990) Mol. Gen. Genet. , vol.222 , pp. 33-36
    • Dassa, E.1
  • 14
    • 0036179213 scopus 로고    scopus 로고
    • Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters
    • Davidson, A. L. 2002. Mechanism of coupling of transport to hydrolysis in bacterial ATP-binding cassette transporters. J. Bacteriol. 184:1225-1233.
    • (2002) J. Bacteriol. , vol.184 , pp. 1225-1233
    • Davidson, A.L.1
  • 15
    • 0027200708 scopus 로고
    • Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system
    • Decker, K., R. Peist, J. Reidl, M. Kossmann, B. Brand, and W. Boos. 1993. Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system. J. Bacteriol. 175:5655-5665.
    • (1993) J. Bacteriol. , vol.175 , pp. 5655-5665
    • Decker, K.1    Peist, R.2    Reidl, J.3    Kossmann, M.4    Brand, B.5    Boos, W.6
  • 16
    • 0031983641 scopus 로고    scopus 로고
    • Negative transcriptional regulation of a positive regulator: The expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc
    • Decker, K., J. Plumbridge, and W. Boos. 1998. Negative transcriptional regulation of a positive regulator: the expression of malT, encoding the transcriptional activator of the maltose regulon of Escherichia coli, is negatively controlled by Mlc. Mol. Microbiol. 27:381-390.
    • (1998) Mol. Microbiol. , vol.27 , pp. 381-390
    • Decker, K.1    Plumbridge, J.2    Boos, W.3
  • 17
    • 28844492475 scopus 로고    scopus 로고
    • The maltodextrin system of Escherichia coli: Glycogen-derived endogenous induction and osmoregulation
    • Dippel, R., T. Bergmiller, A. Böhm, and W. Boos. 2005. The maltodextrin system of Escherichia coli: glycogen-derived endogenous induction and osmoregulation. J. Bacteriol. 187:8332-8339.
    • (2005) J. Bacteriol. , vol.187 , pp. 8332-8339
    • Dippel, R.1    Bergmiller, T.2    Böhm, A.3    Boos, W.4
  • 18
    • 0023394131 scopus 로고
    • Identification of endogenous inducers of the mal system in Escherichia coli
    • Ehrmann, M., and W. Boos. 1987. Identification of endogenous inducers of the mal system in Escherichia coli. J. Bacteriol. 169:3539-3545.
    • (1987) J. Bacteriol. , vol.169 , pp. 3539-3545
    • Ehrmann, M.1    Boos, W.2
  • 19
    • 0032884020 scopus 로고    scopus 로고
    • Glc and is mediated by cAMP levels
    • Glc and is mediated by cAMP levels. Mol. Microbiol. 33:1221-1231.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1221-1231
    • Eppler, T.1    Boos, W.2
  • 20
    • 0036091651 scopus 로고    scopus 로고
    • Glycerol-3-phosphate-induced catabolite repression in Escherichia coli
    • Eppler, T., P. Postma, A. Schütz, U. Völker, and W. Boos. 2002. Glycerol-3-phosphate-induced catabolite repression in Escherichia coli. J. Bacteriol. 184:3044-3052.
    • (2002) J. Bacteriol. , vol.184 , pp. 3044-3052
    • Eppler, T.1    Postma, P.2    Schütz, A.3    Völker, U.4    Boos, W.5
  • 21
    • 0019170188 scopus 로고
    • Methyl-a-maltoside and 5-thiomaltose: Analogs transported by the Escherichia coli maltose transport system
    • Ferenci, T. 1980. Methyl-a-maltoside and 5-thiomaltose: analogs transported by the Escherichia coli maltose transport system. J. Bacteriol. 144:7-11.
    • (1980) J. Bacteriol. , vol.144 , pp. 7-11
    • Ferenci, T.1
  • 22
    • 0019194038 scopus 로고
    • The recognition of maltodextrins by Escherichia coii
    • Ferenci, T. 1980. The recognition of maltodextrins by Escherichia coii. Eur. J. Biochem. 108:631-636.
    • (1980) Eur. J. Biochem. , vol.108 , pp. 631-636
    • Ferenci, T.1
  • 23
    • 0017363137 scopus 로고
    • Energy-coupling of the transport system of Escherichia coli dependent on maltose-binding protein
    • Ferenci, T., W. Boos, M. Schwartz, and S. Szmelcman. 1977. Energy-coupling of the transport system of Escherichia coli dependent on maltose-binding protein. Eur. J. Biochem. 75:187-193.
    • (1977) Eur. J. Biochem. , vol.75 , pp. 187-193
    • Ferenci, T.1    Boos, W.2    Schwartz, M.3    Szmelcman, S.4
  • 24
    • 0018136078 scopus 로고
    • Affinity chromatographic isolation of the periplasmic maltose binding protein
    • Ferenci, T., and U. Klotz. 1978. Affinity chromatographic isolation of the periplasmic maltose binding protein. FEBS Lett. 94:213-217.
    • (1978) FEBS Lett. , vol.94 , pp. 213-217
    • Ferenci, T.1    Klotz, U.2
  • 25
    • 0022525924 scopus 로고
    • Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins
    • Ferenci, T., M. Muir, K.-S. Lee, and D. Maris. 1986. Substrate specificity of the Escherichia coli maltodextrin transport system and its component proteins. Biochim. Biophys. Acta 860:44-50.
    • (1986) Biochim. Biophys. Acta , vol.860 , pp. 44-50
    • Ferenci, T.1    Muir, M.2    Lee, K.-S.3    Maris, D.4
  • 26
    • 0023030937 scopus 로고
    • α-amylase of Escherichia coli, mapping and cloning of the structural gene, malS, and identification of its product as a periplasmic protein
    • Freundlieb, S., and W. Boos. 1986. α-Amylase of Escherichia coli, mapping and cloning of the structural gene, malS, and identification of its product as a periplasmic protein. J. Biol. Chem. 261:2946-2953.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2946-2953
    • Freundlieb, S.1    Boos, W.2
  • 27
    • 0023906938 scopus 로고
    • Facilitated diffusion of p-nitrophenyl-α-D-maltohexaoside through the outer membrane of Escherichia coli
    • Freundlieb, S., U. Ehmann, and W. Boos. 1988. Facilitated diffusion of p-nitrophenyl-α-D-maltohexaoside through the outer membrane of Escherichia coli. J. Biol. Chem. 263:314-320.
    • (1988) J. Biol. Chem. , vol.263 , pp. 314-320
    • Freundlieb, S.1    Ehmann, U.2    Boos, W.3
  • 28
    • 0023883641 scopus 로고
    • Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli
    • Froshauer, S., G. N. Green, D. Boyd, K. McGovern, and J. Beckwith. 1988. Genetic analysis of the membrane insertion and topology of MalF, a cytoplasmic membrane protein of Escherichia coli. J. Mol. Biol. 200:501-511.
    • (1988) J. Mol. Biol. , vol.200 , pp. 501-511
    • Froshauer, S.1    Green, G.N.2    Boyd, D.3    McGovern, K.4    Beckwith, J.5
  • 29
    • 0032544978 scopus 로고    scopus 로고
    • Solution NMR studies of a 42 KDa Escherichia coli maltose binding protein/β-cyclodextrin complex: Chemical shift assignments and analysis
    • Gardner, K. H., X. Zhang, K. Gehring, and L. E. Kay. 1998. Solution NMR studies of a 42 KDa Escherichia coli maltose binding protein/β-cyclodextrin complex: chemical shift assignments and analysis. J. Am. Chem. Soc. 120:11738-11748.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11738-11748
    • Gardner, K.H.1    Zhang, X.2    Gehring, K.3    Kay, L.E.4
  • 30
    • 0034940069 scopus 로고    scopus 로고
    • Solute-binding protein-dependent ABC transporters are responsible for solute efflux in addition to solute uptake
    • Hosie, A. H. F., D. Allaway, M. A. Jones, D. L. Walshaw, A. W. B. Johnston, and P. S. Poole. 2001. Solute-binding protein-dependent ABC transporters are responsible for solute efflux in addition to solute uptake. Mol. Microbiol. 40:1449-1459.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1449-1459
    • Hosie, A.H.F.1    Allaway, D.2    Jones, M.A.3    Walshaw, D.L.4    Johnston, A.W.B.5    Poole, P.S.6
  • 31
    • 4043050193 scopus 로고    scopus 로고
    • MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding
    • Joly, N., A. Bohm, W. Boos, and E. Richet. 2004. MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding. J. Biol. Chem. 279:33123-33130.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33123-33130
    • Joly, N.1    Bohm, A.2    Boos, W.3    Richet, E.4
  • 32
    • 0016151381 scopus 로고
    • Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein
    • Kellermann, O., and S. Szmelcman. 1974. Active transport of maltose in Escherichia coli K12. Involvement of a "periplasmic" maltose binding protein. Eur. J. Biochem. 47:139-149.
    • (1974) Eur. J. Biochem. , vol.47 , pp. 139-149
    • Kellermann, O.1    Szmelcman, S.2
  • 33
    • 0025904264 scopus 로고
    • The activities of the Escherichia coli MaIK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations
    • Kühnau, S., M. Reyes, A. Sievertsen, H. A. Shuman, and W. Boos. 1991. The activities of the Escherichia coli MaIK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations. J. Bacteriol. 173:2180-2186.
    • (1991) J. Bacteriol. , vol.173 , pp. 2180-2186
    • Kühnau, S.1    Reyes, M.2    Sievertsen, A.3    Shuman, H.A.4    Boos, W.5
  • 34
    • 0034675992 scopus 로고    scopus 로고
    • Signal transduction between a membrane bound transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli
    • Lee, S.-J., W. Boos, J.-P. Bouché, and J. Plumbridge. 2000. Signal transduction between a membrane bound transporter, PtsG, and a soluble transcription factor, Mlc, of Escherichia coli. EMBO J. 19:5353-5361.
    • (2000) EMBO J. , vol.19 , pp. 5353-5361
    • Lee, S.-J.1    Boos, W.2    Bouché, J.-P.3    Plumbridge, J.4
  • 35
    • 0033060579 scopus 로고    scopus 로고
    • The identification of a new family of sugar efflux pumps in Escherichia coli
    • Liu, J. Y., P. F. Miller, M. Gosink, and E. R. Olson. 1999. The identification of a new family of sugar efflux pumps in Escherichia coli. Mol. Microbiol. 31:1845-1851.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1845-1851
    • Liu, J.Y.1    Miller, P.F.2    Gosink, M.3    Olson, E.R.4
  • 36
    • 0040436094 scopus 로고    scopus 로고
    • Functional and biochemical characterization of Escherichia coli sugar efflux transporters
    • Liu, J. Y., P. F. Miller, J. Willard, and E. R. Olson. 1999. Functional and biochemical characterization of Escherichia coli sugar efflux transporters. J. Biol. Chem. 274:22977-22984.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22977-22984
    • Liu, J.Y.1    Miller, P.F.2    Willard, J.3    Olson, E.R.4
  • 37
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 38
    • 0024853842 scopus 로고
    • Energy coupling to periplasmic binding protein-dependent transport systems: Stoichiometry of ATP hydrolysis during transport in vivo
    • Mimmack, M. L., M. P. Gallagher, S. R. Pearce, S. C. Hyde, I. R. Booth, and C. F. Higgins. 1989. Energy coupling to periplasmic binding protein-dependent transport systems: stoichiometry of ATP hydrolysis during transport in vivo. Proc. Natl. Acad. Sci. USA 86:8257-8261.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8257-8261
    • Mimmack, M.L.1    Gallagher, M.P.2    Pearce, S.R.3    Hyde, S.C.4    Booth, I.R.5    Higgins, C.F.6
  • 39
    • 0010441837 scopus 로고
    • De l'amylomaltase d'Escherichia coli
    • Monod, J., and A. M. Torriani. 1950. De l'amylomaltase d'Escherichia coli. Ann. Inst. Pasteur 78:65-77.
    • (1950) Ann. Inst. Pasteur , vol.78 , pp. 65-77
    • Monod, J.1    Torriani, A.M.2
  • 40
    • 0027272354 scopus 로고
    • The ATP-binding cassette (ABC) transporter for maltose/maltodextrins of Salmonella typhimurium. Characterization of the ATPase activity associated with the purified MalK subunit
    • Morbach, S., S. Tebbe, and E. Schneider. 1993. The ATP-binding cassette (ABC) transporter for maltose/maltodextrins of Salmonella typhimurium. Characterization of the ATPase activity associated with the purified MalK subunit. J. Biol. Chem. 268:18617-18621.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18617-18621
    • Morbach, S.1    Tebbe, S.2    Schneider, E.3
  • 41
    • 0030910930 scopus 로고    scopus 로고
    • Subunit interactions in ABC transporters: A conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits
    • Mourez, M., M. Hofnung, and E. Dassa. 1997. Subunit interactions in ABC transporters: a conserved sequence in hydrophobic membrane proteins of periplasmic permeases defines an important site of interaction with the ATPase subunits. EMBO J. 16:3066-3077.
    • (1997) EMBO J. , vol.16 , pp. 3066-3077
    • Mourez, M.1    Hofnung, M.2    Dassa, E.3
  • 42
    • 0021925495 scopus 로고
    • Influence of transport energization on the growth yield of Escherichia coli
    • Muir, M., L. Williams, and T. Ferenci. 1985. Influence of transport energization on the growth yield of Escherichia coli. J. Bacteriol. 163:1237-1242.
    • (1985) J. Bacteriol. , vol.163 , pp. 1237-1242
    • Muir, M.1    Williams, L.2    Ferenci, T.3
  • 43
    • 0032004274 scopus 로고    scopus 로고
    • 14C]-maltose using amylomaltase, cyclodextrin glucosyltransferase, and cyclodextrinase
    • 14C]-maltose using amylomaltase, cyclodextrin glucosyltransferase, and cyclodextrinase. Carbohydr. Res. 307:375-378.
    • (1998) Carbohydr. Res. , vol.307 , pp. 375-378
    • Pajatsch, M.1    Böck, A.2    Boos, W.3
  • 44
    • 0017082211 scopus 로고
    • The action pattern of amylomaltase from Escherichia coli
    • Palmer, N. T., B. E. Ryman, and W. J. Whelan. 1976. The action pattern of amylomaltase from Escherichia coli. Eur. J. Biochem. 69:105-115.
    • (1976) Eur. J. Biochem. , vol.69 , pp. 105-115
    • Palmer, N.T.1    Ryman, B.E.2    Whelan, W.J.3
  • 45
    • 17544372725 scopus 로고    scopus 로고
    • The MalT-dependent and malZ-encoded maltodextrin glucosidase of Escherichia coli can be converted into a dextrinyltransferase by a single mutation
    • Peist, H., C. Schneider-Fresenius, and W. Boos. 1996. The MalT-dependent and malZ-encoded maltodextrin glucosidase of Escherichia coli can be converted into a dextrinyltransferase by a single mutation. J. Biol. Chem. 271:10681-10689.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10681-10689
    • Peist, H.1    Schneider-Fresenius, C.2    Boos, W.3
  • 46
    • 0001014412 scopus 로고    scopus 로고
    • Phosphoenolpyruvate: Carbohydrate phosphotransferase system
    • F. C. Neidhardt, R. Curtiss, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.). American Society for Microbiology, Washington, D.C.
    • Postma, P. W., J. W. Lengeler, and G. R. Jacobson. 1996. Phosphoenolpyruvate: carbohydrate phosphotransferase system, p. 1149-1174. In F. C. Neidhardt, R. Curtiss, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, 2nd ed., vol. 1. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 1149-1174
    • Postma, P.W.1    Lengeler, J.W.2    Jacobson, G.R.3
  • 47
    • 0024042231 scopus 로고
    • Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase
    • Pugsley, A. P., and C. Dubreuil. 1988. Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase. Mol. Microbiol. 2:473-479.
    • (1988) Mol. Microbiol. , vol.2 , pp. 473-479
    • Pugsley, A.P.1    Dubreuil, C.2
  • 49
    • 0023192487 scopus 로고
    • Maltotriose is the inducer of the maltose regulon
    • Raibaud, O., and E. Richet. 1987. Maltotriose is the inducer of the maltose regulon. J. Bacteriol. 169:3059-3061.
    • (1987) J. Bacteriol. , vol.169 , pp. 3059-3061
    • Raibaud, O.1    Richet, E.2
  • 50
    • 0024594574 scopus 로고
    • A complex nucleoprotein structure involved in activation of transcription of two divergent Escherichia coli promoters
    • Raibaud, O., D. Vidal-Ingigliardi, and E. Richet. 1989. A complex nucleoprotein structure involved in activation of transcription of two divergent Escherichia coli promoters. J. Mol. Biol. 205:471-485.
    • (1989) J. Mol. Biol. , vol.205 , pp. 471-485
    • Raibaud, O.1    Vidal-Ingigliardi, D.2    Richet, E.3
  • 51
    • 0015713398 scopus 로고
    • Isolation of the bacteriophage lambda receptor from Escherichia coli
    • Randall-Hazelbauer, L., and M. Schwartz. 1973. Isolation of the bacteriophage lambda receptor from Escherichia coli. J. Bacteriol. 116:1436-1446.
    • (1973) J. Bacteriol. , vol.116 , pp. 1436-1446
    • Randall-Hazelbauer, L.1    Schwartz, M.2
  • 52
    • 0022456176 scopus 로고
    • Transport of p-nitrophenyl-α-maltoside by the maltose transport system of Escherichia coli and its subsequent hydrolysis by a cytoplasmic maltosidase
    • Reyes, M., N. A. Treptow, and H. A. Shuman. 1986. Transport of p-nitrophenyl-α-maltoside by the maltose transport system of Escherichia coli and its subsequent hydrolysis by a cytoplasmic maltosidase. J. Bacteriol. 165:918-922.
    • (1986) J. Bacteriol. , vol.165 , pp. 918-922
    • Reyes, M.1    Treptow, N.A.2    Shuman, H.A.3
  • 53
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer, T., T. A. Keller, Y. F. Wang, and J. P. Rosenbusch. 1995. Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267:512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 54
    • 0026703159 scopus 로고
    • Molecular characterization of the MalT-dependent periplasmic α-amylase of Escherichia coli encoded by malS
    • Schneider, E., S. Freundlieb, S. Tapio, and W. Boos. 1992. Molecular characterization of the MalT-dependent periplasmic α-amylase of Escherichia coli encoded by malS. J. Biol. Chem. 267:5148-5154.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5148-5154
    • Schneider, E.1    Freundlieb, S.2    Tapio, S.3    Boos, W.4
  • 55
    • 0000706936 scopus 로고
    • The maltose regulon
    • F. C. Neidhardt (ed.). American Society for Microbiology, Washington, D.C.
    • Schwartz, M. 1987. The maltose regulon, p. 1482-1502. In F. C. Neidhardt (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology, vol. 2. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , vol.2 , pp. 1482-1502
    • Schwartz, M.1
  • 56
    • 0014133549 scopus 로고
    • La maltodextrin phosphorylase d'Escherichia coli
    • Schwartz, M., and M. Hofnung. 1967. La maltodextrin phosphorylase d'Escherichia coli. Eur. J. Biochem. 2:132-145.
    • (1967) Eur. J. Biochem. , vol.2 , pp. 132-145
    • Schwartz, M.1    Hofnung, M.2
  • 57
    • 0030606240 scopus 로고    scopus 로고
    • Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: The maltose-, glucose/galactose- and ribose-binding proteins
    • Shilton, B. H., M. M. Flocco, M. Nilsson, and S. L. Mowbray. 1996. Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: the maltose-, glucose/galactose- and ribose-binding proteins. J. Mol. Biol. 264:350-363.
    • (1996) J. Mol. Biol. , vol.264 , pp. 350-363
    • Shilton, B.H.1    Flocco, M.M.2    Nilsson, M.3    Mowbray, S.L.4
  • 58
    • 0019464719 scopus 로고
    • Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system
    • Shuman, H. A., and T. J. Silhavy. 1981. Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system. J. Biol. Chem. 256:560-562.
    • (1981) J. Biol. Chem. , vol.256 , pp. 560-562
    • Shuman, H.A.1    Silhavy, T.J.2
  • 59
    • 0025754301 scopus 로고
    • The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., G.-Y. Lu, and F. A. Quiocho. 1991. The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266:5202-5219.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3
  • 60
    • 0017127269 scopus 로고
    • Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and λ-resistant mutants with the dissociation constants of the maltose binding protein as measured by fluorescence quenching
    • Szmelcman, S., M. Schwartz, T. J. Silhavy, and W. Boos. 1976. Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and λ-resistant mutants with the dissociation constants of the maltose binding protein as measured by fluorescence quenching. Eur. J. Biochem. 65:13-19.
    • (1976) Eur. J. Biochem. , vol.65 , pp. 13-19
    • Szmelcman, S.1    Schwartz, M.2    Silhavy, T.J.3    Boos, W.4
  • 61
    • 0025985499 scopus 로고
    • The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase
    • Tapio, S., F. Yeh, H. A. Shuman, and W. Boos. 1991. The malZ gene of Escherichia coli, a member of the maltose regulon, encodes a maltodextrin glucosidase. J. Biol. Chem. 266:19450-19458.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19450-19458
    • Tapio, S.1    Yeh, F.2    Shuman, H.A.3    Boos, W.4
  • 62
    • 0022794836 scopus 로고
    • 3-Azi-1-methoxybutyl D-maltooligosaccharides specifically bind to the maltose/maltooligosaccharide-binding protein of Escherichia coli and can be used as photoaffinity labels
    • Thieme, R., H. Lay, A. Oser, J. Lehmann, S. Wrissenberg, and W. Boos. 1986. 3-Azi-1-methoxybutyl D-maltooligosaccharides specifically bind to the maltose/maltooligosaccharide-binding protein of Escherichia coli and can be used as photoaffinity labels. Eur. J. Biochem. 160:83-91.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 83-91
    • Thieme, R.1    Lay, H.2    Oser, A.3    Lehmann, J.4    Wrissenberg, S.5    Boos, W.6
  • 63
    • 0018703721 scopus 로고
    • Escherichia coli mutants impaired in maltodextrin transport
    • Wandersman, C., M. Schwartz, and T. Ferenci. 1979. Escherichia coli mutants impaired in maltodextrin transport. J. Bacteriol. 140:1-13.
    • (1979) J. Bacteriol. , vol.140 , pp. 1-13
    • Wandersman, C.1    Schwartz, M.2    Ferenci, T.3
  • 64
    • 0031014875 scopus 로고    scopus 로고
    • The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase
    • Watson, K. A., R. Schinzel, D. Palm, and L. N. Johnson. 1997. The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase. EMBO J. 16:1-14.
    • (1997) EMBO J. , vol.16 , pp. 1-14
    • Watson, K.A.1    Schinzel, R.2    Palm, D.3    Johnson, L.N.4
  • 65
    • 2642638300 scopus 로고
    • The characterization of the pathway of maltose utilization by Escherichia coli. I. Purification and physical chemical properties of the enzyme amylomaltase
    • Wiesmeyer, H., and M. Cohn. 1960. The characterization of the pathway of maltose utilization by Escherichia coli. I. Purification and physical chemical properties of the enzyme amylomaltase. Biochim. Biophys. Acta 39:417-426.
    • (1960) Biochim. Biophys. Acta , vol.39 , pp. 417-426
    • Wiesmeyer, H.1    Cohn, M.2
  • 66
    • 1842271033 scopus 로고
    • The characterization of the pathway of maltose utilization by Escherichia coli. II. General properties and mechanism of action of amylomaltase
    • Wiesmeyer, H., and M. Cohn. 1960. The characterization of the pathway of maltose utilization by Escherichia coli. II. General properties and mechanism of action of amylomaltase. Biochim. Biophys. Acta 39:427-439.
    • (1960) Biochim. Biophys. Acta , vol.39 , pp. 427-439
    • Wiesmeyer, H.1    Cohn, M.2


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