메뉴 건너뛰기




Volumn 20, Issue 10, 2001, Pages 2480-2486

The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor

Author keywords

Dihydroxyacetone kinase; Phosphohistidine; Protein phosphorylation; PTS

Indexed keywords

ADENOSINE TRIPHOSPHATE; CARBOHYDRATE; DIHYDROXYACETONE KINASE; MANNOSE; PHOSPHOENOLPYRUVATE; PHOSPHOPROTEIN; PHOSPHOTRANSFERASE; PROTEIN DHAL; PROTEIN DHAM; PROTEIN SUBUNIT; SUGAR; UNCLASSIFIED DRUG;

EID: 0035873544     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/20.10.2480     Document Type: Article
Times cited : (98)

References (37)
  • 1
    • 0024462409 scopus 로고
    • Protein phosphorylation regulates transcription of the β-glucoside utilization operon in E. coli
    • Amster-Choder, O., Houman, F. and Wright, A. (1989) Protein phosphorylation regulates transcription of the β-glucoside utilization operon in E. coli. Cell, 58, 847-855.
    • (1989) Cell , vol.58 , pp. 847-855
    • Amster-Choder, O.1    Houman, F.2    Wright, A.3
  • 3
    • 0034652155 scopus 로고    scopus 로고
    • Folding and activity of circularly permuted forms of a polytopic membrane protein
    • Beutler, R., Ruggiero, F. and Erni, B. (2000) Folding and activity of circularly permuted forms of a polytopic membrane protein. Proc. Natl Acad. Sci. USA, 97, 1477-1482.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1477-1482
    • Beutler, R.1    Ruggiero, F.2    Erni, B.3
  • 4
    • 0035131757 scopus 로고    scopus 로고
    • Heterodimeric dihydroxyacetone kinase from a ptsI mutant of Escherichia coli
    • Beutler, R., Kämpfer, U., Schaller, J. and Erni, B. (2001) Heterodimeric dihydroxyacetone kinase from a ptsI mutant of Escherichia coli. Microbiology, 147, 249-250.
    • (2001) Microbiology , vol.147 , pp. 249-250
    • Beutler, R.1    Kämpfer, U.2    Schaller, J.3    Erni, B.4
  • 5
    • 0026670148 scopus 로고
    • The glucose transporter of Escherichia coli. Mutants with impaired translocation activity that retain phosphorylation activity
    • Buhr, A., Daniels, G.A. and Erni, B. (1992) The glucose transporter of Escherichia coli. Mutants with impaired translocation activity that retain phosphorylation activity. J. Biol. Chem., 267, 3847-3851.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3847-3851
    • Buhr, A.1    Daniels, G.A.2    Erni, B.3
  • 6
    • 0029083167 scopus 로고
    • Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii
    • Daniel, R., Stuertz, K. and Gottschalk, G. (1995) Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii. J. Bacteriol., 177, 4392-4401.
    • (1995) J. Bacteriol. , vol.177 , pp. 4392-4401
    • Daniel, R.1    Stuertz, K.2    Gottschalk, G.3
  • 7
    • 0023654528 scopus 로고
    • The mannose permease of Escherichia coli consists of three different proteins: Amino-acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage λ DNA
    • Erni, B., Zanolari, B. and Kocher, H.P. (1987) The mannose permease of Escherichia coli consists of three different proteins: amino-acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage λ DNA. J. Biol. Chem., 262, 5238-5247.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5238-5247
    • Erni, B.1    Zanolari, B.2    Kocher, H.P.3
  • 8
    • 0024418122 scopus 로고
    • Mannose permease of Escherichia coli. Domain structure and function of the phosphorylating subunit
    • Erni, B., Zanolari, B., Graff, P. and Kocher, H.P. (1989) Mannose permease of Escherichia coli. Domain structure and function of the phosphorylating subunit. J. Biol. Chem., 264, 18733-18741.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18733-18741
    • Erni, B.1    Zanolari, B.2    Graff, P.3    Kocher, H.P.4
  • 9
    • 0345299162 scopus 로고    scopus 로고
    • Catabolite control of Escherichia coli regulatory protein Bg1g activity by antagonistically acting phosphorylations
    • Görke, B. and Rak, B. (1999) Catabolite control of Escherichia coli regulatory protein Bg1G activity by antagonistically acting phosphorylations. EMBO J., 18, 3370-3379.
    • (1999) EMBO J. , vol.18 , pp. 3370-3379
    • Görke, B.1    Rak, B.2
  • 10
    • 0024677030 scopus 로고
    • Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12
    • Gutierrez, C., Ardourel, M., Bremer, E., Middendorf, A., Boos, W. and Ehmann, U. (1989) Analysis and DNA sequence of the osmoregulated treA gene encoding the periplasmic trehalase of Escherichia coli K12. Mol. Gen. Genet., 217, 347-354.
    • (1989) Mol. Gen. Genet. , vol.217 , pp. 347-354
    • Gutierrez, C.1    Ardourel, M.2    Bremer, E.3    Middendorf, A.4    Boos, W.5    Ehmann, U.6
  • 12
    • 0342443314 scopus 로고
    • Group translocation transport systems
    • Rosen, B. (ed.), Marcel Dekker, New York, NY
    • Hays, J.B. (1978) Group translocation transport systems. In Rosen, B. (ed.), Bacterial Transport. Marcel Dekker, New York, NY, pp. 43-102.
    • (1978) Bacterial Transport. , pp. 43-102
    • Hays, J.B.1
  • 13
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K. and Pease, L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 14
    • 0034609791 scopus 로고    scopus 로고
    • The large-scale organization of metabolic networks
    • Jeong, H., Tombor, B., Albert, R., Oltvai, Z.N. and Barabasi, A.L. (2000) The large-scale organization of metabolic networks. Nature, 407, 651-654.
    • (2000) Nature , vol.407 , pp. 651-654
    • Jeong, H.1    Tombor, B.2    Albert, R.3    Oltvai, Z.N.4    Barabasi, A.L.5
  • 15
    • 0021362573 scopus 로고
    • An inducible phosphoenolpyruvate: Dihydroxyacetone phosphotransferase system in Escherichia coli
    • Jin, R.Z. and Lin, E.C.C. (1984) An inducible phosphoenolpyruvate: dihydroxyacetone phosphotransferase system in Escherichia coli. J. Gen. Microbiol., 130, 83-88.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 83-88
    • Jin, R.Z.1    Lin, E.C.C.2
  • 16
    • 0021170123 scopus 로고
    • Purification and properties of dihydroxyacetone kinase from Klebsiella pneumoniae
    • Johnson, E.A., Burke, S.K., Forage, R.G. and Lin, E.C. (1984) Purification and properties of dihydroxyacetone kinase from Klebsiella pneumoniae. J. Bacteriol., 160, 55-60.
    • (1984) J. Bacteriol. , vol.160 , pp. 55-60
    • Johnson, E.A.1    Burke, S.K.2    Forage, R.G.3    Lin, E.C.4
  • 17
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley, L.A., MacCallum, R.M. and Sternberg, M.J. (2000) Enhanced genome annotation using structural profiles in the program 3D-PSSM. J. Mol. Biol., 299, 499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 18
    • 0000186326 scopus 로고
    • Phosphate bound to histidine in protein as an intermediate in a novel phosphotransferase system
    • Kundig, W., Gosh, S. and Roseman, S. (1964) Phosphate bound to histidine in protein as an intermediate in a novel phosphotransferase system. Proc. Natl Acad. Sci. USA, 52, 1067-1074.
    • (1964) Proc. Natl Acad. Sci. USA , vol.52 , pp. 1067-1074
    • Kundig, W.1    Gosh, S.2    Roseman, S.3
  • 19
    • 0028534956 scopus 로고
    • Enzymes II of the phosphoenolpyruvate-dependent phosphotransferase systems: Their structure and function in carbohydrate transport
    • Lengeler, J.W., Jahreis, K. and Wehmeier, U.F. (1994) Enzymes II of the phosphoenolpyruvate-dependent phosphotransferase systems: their structure and function in carbohydrate transport. Biochim. Biophys. Acta, 1188, 1-28.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 1-28
    • Lengeler, J.W.1    Jahreis, K.2    Wehmeier, U.F.3
  • 20
    • 0030586030 scopus 로고    scopus 로고
    • The first step in sugar transport: Crystal structure of the amino terminal domain of enzyme I of the E.coli PEP:Sugar phosphotransferase system and a model of the phosphotransfer complex with HPr
    • Liao, D.I., Silverton, E., Seok, Y.J., Lee, B.R., Peterkofsky, A. and Davies, D.R. (1996) The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E.coli PEP:sugar phosphotransferase system and a model of the phosphotransfer complex with HPr. Structure, 4, 861-872.
    • (1996) Structure , vol.4 , pp. 861-872
    • Liao, D.I.1    Silverton, E.2    Seok, Y.J.3    Lee, B.R.4    Peterkofsky, A.5    Davies, D.R.6
  • 21
    • 0026043235 scopus 로고
    • Sugar transport by the bacterial phosphotransferase system. Structural and thermodynamic domains of enzyme I of Salmonella typhimurium
    • LiCalsi, C., Crocenzi, T.S., Freire, E. and Roseman, S. (1991) Sugar transport by the bacterial phosphotransferase system. Structural and thermodynamic domains of enzyme I of Salmonella typhimurium. J. Biol. Chem., 266, 19519-19527.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19519-19527
    • LiCalsi, C.1    Crocenzi, T.S.2    Freire, E.3    Roseman, S.4
  • 22
    • 0029120342 scopus 로고
    • A string of enzymes, purification and characterization of a fusion protein comprising the four subunits of the glucose phosphotransferase system of Escherichia coli
    • Mao, Q., Schunk, T., Gerber, B. and Erni, B. (1995) A string of enzymes, purification and characterization of a fusion protein comprising the four subunits of the glucose phosphotransferase system of Escherichia coli. J. Biol. Chem., 270, 18295-18300.
    • (1995) J. Biol. Chem. , vol.270 , pp. 18295-18300
    • Mao, Q.1    Schunk, T.2    Gerber, B.3    Erni, B.4
  • 23
    • 0028111080 scopus 로고
    • Independent folding of the domains in the hydrophilic subunit IIAB(man) of the mannose transporter of Escherichia coli
    • Markovic-Housley, Z., Cooper, A., Lustig, A., Flükiger, K., Stolz, B. and Erni, B. (1994) Independent folding of the domains in the hydrophilic subunit IIAB(man) of the mannose transporter of Escherichia coli. Biochemistry, 33, 10977-10984.
    • (1994) Biochemistry , vol.33 , pp. 10977-10984
    • Markovic-Housley, Z.1    Cooper, A.2    Lustig, A.3    Flükiger, K.4    Stolz, B.5    Erni, B.6
  • 24
    • 0030886370 scopus 로고    scopus 로고
    • Phage display selection of peptides against enzyme I of the phosphoenolpyruvate sugar phosphotransferase system (PTS)
    • Mukhija, S. and Erni, B. (1997) Phage display selection of peptides against enzyme I of the phosphoenolpyruvate sugar phosphotransferase system (PTS). Mol. Microbiol., 25, 1159-1166.
    • (1997) Mol. Microbiol. , vol.25 , pp. 1159-1166
    • Mukhija, S.1    Erni, B.2
  • 26
    • 0023944928 scopus 로고
    • Glucose permease of Escherichia coli. The effect of cysteine to serine mutations on the function, stability, and regulation of transport and phosphorylation
    • Nuoffer, C., Zanolari, B. and Erni, B. (1988) Glucose permease of Escherichia coli. The effect of cysteine to serine mutations on the function, stability, and regulation of transport and phosphorylation. J. Biol. Chem., 263, 6647-6655.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6647-6655
    • Nuoffer, C.1    Zanolari, B.2    Erni, B.3
  • 27
    • 0033759438 scopus 로고    scopus 로고
    • Functional genomic studies of dihydroxyacetone utilization in Escherichia coli
    • Paulsen, I.T., Reizer, J., Jin, R.Z., Lin, E.C. and Saier, M.H. (2000) Functional genomic studies of dihydroxyacetone utilization in Escherichia coli. Microbiology, 146, 2343-2344.
    • (2000) Microbiology , vol.146 , pp. 2343-2344
    • Paulsen, I.T.1    Reizer, J.2    Jin, R.Z.3    Lin, E.C.4    Saier, M.H.5
  • 29
    • 0033045836 scopus 로고    scopus 로고
    • Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system
    • Robillard, G.T. and Broos, J. (1999) Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system. Biochim. Biophys. Acta, 1422, 73-104.
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 73-104
    • Robillard, G.T.1    Broos, J.2
  • 30
    • 0024997263 scopus 로고
    • Adaptation of Salmonella typhimurium mutants containing uncoupled enzyme IIGlc to glucose-limited conditions
    • Ruijter, G.J.G., Postma, P.W. and van Dam, K. (1990) Adaptation of Salmonella typhimurium mutants containing uncoupled enzyme IIGlc to glucose-limited conditions. J. Bacteriol., 172, 4783-4789.
    • (1990) J. Bacteriol. , vol.172 , pp. 4783-4789
    • Ruijter, G.J.G.1    Postma, P.W.2    Van Dam, K.3
  • 31
    • 0026708450 scopus 로고
    • Analysis of mutations that uncouple transport from phosphorylation in enzyme-IIGlc of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system
    • Ruijter, G.J.G., van Meurs, G., Verwey, M.A., Postma, P.W. and van Dam, K. (1992) Analysis of mutations that uncouple transport from phosphorylation in enzyme-IIGlc of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system. J. Bacteriol., 174, 2843-2850.
    • (1992) J. Bacteriol. , vol.174 , pp. 2843-2850
    • Ruijter, G.J.G.1    Van Meurs, G.2    Verwey, M.A.3    Postma, P.W.4    Van Dam, K.5
  • 32
    • 0026546539 scopus 로고
    • Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenol-pyruvate:Sugar phosphotransferase system
    • Saier, M.H. and Reizer, J. (1992) Proposed uniform nomenclature for the proteins and protein domains of the bacterial phosphoenol-pyruvate:sugar phosphotransferase system. J. Bacteriol., 174, 1433-1438.
    • (1992) J. Bacteriol. , vol.174 , pp. 1433-1438
    • Saier, M.H.1    Reizer, J.2
  • 34
    • 0025366839 scopus 로고
    • β-glucoside permease represses the bgl operon of Escherichia coli by phosphorylation of the antiterminator protein and also interacts with glucose-specific enzyme III, the key element in catabolite control
    • Schnetz, K. and Rak, B. (1990) β-glucoside permease represses the bgl operon of Escherichia coli by phosphorylation of the antiterminator protein and also interacts with glucose-specific enzyme III, the key element in catabolite control. Proc. Natl Acad. Sci. USA, 87, 5074-5078.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5074-5078
    • Schnetz, K.1    Rak, B.2
  • 35
    • 0031808469 scopus 로고    scopus 로고
    • PRD - A protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria
    • Stulke, J., Arnaud, M., Rapoport, G. and Martin-Verstraete, I. (1998) PRD - a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria. Mol. Microbiol., 28, 865-874.
    • (1998) Mol. Microbiol. , vol.28 , pp. 865-874
    • Stulke, J.1    Arnaud, M.2    Rapoport, G.3    Martin-Verstraete, I.4
  • 36
    • 0021964555 scopus 로고
    • Intracellular phosphorylation of glucose analogs via the phosphoenolpyruvate:Mannose phosphotransferase system in Streptococcus lactis
    • Thompson, J. and Chassy, B.M. (1985) Intracellular phosphorylation of glucose analogs via the phosphoenolpyruvate:mannose phosphotransferase system in Streptococcus lactis. J. Bacteriol., 162, 224-234.
    • (1985) J. Bacteriol. , vol.162 , pp. 224-234
    • Thompson, J.1    Chassy, B.M.2
  • 37
    • 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. and Saier, M.H. (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, M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.