메뉴 건너뛰기




Volumn 43, Issue 21, 2004, Pages 6387-6392

Identifying latent enzyme activities: Substrate ambiguity within modern bacterial sugar kinases

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; DNA; FUNCTIONS; GENES; GLUCOSE; METABOLISM;

EID: 2542594077     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049424m     Document Type: Article
Times cited : (87)

References (44)
  • 1
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R. A. (1976) Enzyme recruitment in evolution of new function, Annu. Rev. Microbiol. 30, 409-425.
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 4
    • 0017058392 scopus 로고
    • Evolution of enzyme function and the development of catalytic efficiency
    • Albery, W. J., and Knowles, J. R. (1976) Evolution of enzyme function and the development of catalytic efficiency, Biochemistry 15, 5631-5640.
    • (1976) Biochemistry , vol.15 , pp. 5631-5640
    • Albery, W.J.1    Knowles, J.R.2
  • 5
    • 0024388720 scopus 로고
    • Evolutionary optimization of the catalytic effectiveness of an enzyme
    • Burbaum, J. J., Raines, R. T., Albery, W. J., and Knowles, J. R. (1989) Evolutionary optimization of the catalytic effectiveness of an enzyme, Biochemistry 28, 9293-9305.
    • (1989) Biochemistry , vol.28 , pp. 9293-9305
    • Burbaum, J.J.1    Raines, R.T.2    Albery, W.J.3    Knowles, J.R.4
  • 6
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signaling
    • Blume-Jensen, P., and Hunter, T. (2001) Oncogenic kinase signaling, Nature 411, 355-365.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 7
    • 84892166712 scopus 로고
    • Einfluss der configuration auf die wirkung derenzyme
    • Fischer, E. (1894) Einfluss der configuration auf die wirkung derenzyme, Ber. Dtsch. Chem. Ges. 27, 2985-2993.
    • (1894) Ber. Dtsch. Chem. Ges. , vol.27 , pp. 2985-2993
    • Fischer, E.1
  • 8
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein synthesis
    • Koshland, D. E., Jr. (1958) Application of a theory of enzyme specificity to protein synthesis, Proc. Natl. Acad. Sci. U.S.A. 44, 98-104.
    • (1958) Proc. Natl. Acad. Sci. U.S.A. , vol.44 , pp. 98-104
    • Koshland Jr., D.E.1
  • 9
    • 0014902337 scopus 로고
    • The evolution of bacterial enzyme systems
    • Hegeman, G. D., and Rosenberg, S. L. (1970) The evolution of bacterial enzyme systems, Annu. Rev. Microbiol. 24, 429-462.
    • (1970) Annu. Rev. Microbiol. , vol.24 , pp. 429-462
    • Hegeman, G.D.1    Rosenberg, S.L.2
  • 10
    • 0037952253 scopus 로고
    • Evolution of a catabolic pathway in bacteria
    • Lerner, S. A., Wu, T. T., and Lin, E. C. C. (1964) Evolution of a catabolic pathway in bacteria, Science 146, 1313-1315.
    • (1964) Science , vol.146 , pp. 1313-1315
    • Lerner, S.A.1    Wu, T.T.2    Lin, E.C.C.3
  • 11
    • 0013794971 scopus 로고
    • A basis for the utilization of unnatural pentoses and pentitols by Aerobacter aerogenes
    • Mortlock, R. P., Fossitt, D. D., and Wood, W. A. (1965) A basis for the utilization of unnatural pentoses and pentitols by Aerobacter aerogenes, Proc. Natl. Acad. Sci. U.S.A. 54, 572-579.
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 572-579
    • Mortlock, R.P.1    Fossitt, D.D.2    Wood, W.A.3
  • 12
    • 0342517635 scopus 로고
    • Evolution of a second gene for β-galactosidase in Escherichia coli
    • Campbell, J. H., Lengyel, J. A., and Langridge, J. (1973) Evolution of a second gene for β-galactosidase in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 70, 1841-1845.
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 1841-1845
    • Campbell, J.H.1    Lengyel, J.A.2    Langridge, J.3
  • 14
    • 0016144587 scopus 로고
    • Gene duplication in experimental enzyme evolution
    • Rigby, P. W. J., Burleigh, B. D., Jr., and Hartley, B. S. (1974) Gene duplication in experimental enzyme evolution, Nature 251, 200-204.
    • (1974) Nature , vol.251 , pp. 200-204
    • Rigby, P.W.J.1    Burleigh Jr., B.D.2    Hartley, B.S.3
  • 15
    • 0017129243 scopus 로고
    • Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophase λ and μ
    • Casadaban, M. J. (1976) Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophase λ and μ, J. Mol. Biol. 104, 541-555.
    • (1976) J. Mol. Biol. , vol.104 , pp. 541-555
    • Casadaban, M.J.1
  • 16
    • 0025022359 scopus 로고
    • Cyclic AMP synthesis in Escherichia coli strains bearing known deletions in the pts phosphotranferase operon
    • Levy, S., Zeng, G.-Q., and Danchin, A. (1990) Cyclic AMP synthesis in Escherichia coli strains bearing known deletions in the pts phosphotranferase operon, Gene 86, 27-33.
    • (1990) Gene , vol.86 , pp. 27-33
    • Levy, S.1    Zeng, G.-Q.2    Danchin, A.3
  • 17
  • 18
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Miller, J. H. (1972) Experiments in Molecular Genetics, pp 201-205, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1972) Experiments in Molecular Genetics , pp. 201-205
    • Miller, J.H.1
  • 19
    • 84955554260 scopus 로고
    • Lactose-fermenting bacteria in faeces
    • MacConkey, A. (1905) Lactose-fermenting bacteria in faeces, J. Hyg. 5, 333-379.
    • (1905) J. Hyg. , vol.5 , pp. 333-379
    • MacConkey, A.1
  • 20
    • 0014748661 scopus 로고
    • Potassium-dependent mutants of Escherichia coli K-12
    • Epstein, W., and Davies, M. (1970) Potassium-dependent mutants of Escherichia coli K-12, J. Bacteriol. 101, 836-843.
    • (1970) J. Bacteriol. , vol.101 , pp. 836-843
    • Epstein, W.1    Davies, M.2
  • 22
    • 0028949495 scopus 로고
    • Characterization of the Zymomonas mobilis glucose facilitator gene product (glf) in recombinant Escherichia coli: Examination of transport mechanism, kinetics, and the role of glucose in glucose transport
    • Parker, C., Barnell, W. O., Snoep, J. L., Ingram, L. O., and Conway, T. (1995) Characterization of the Zymomonas mobilis glucose facilitator gene product (glf) in recombinant Escherichia coli: Examination of transport mechanism, kinetics, and the role of glucose in glucose transport, Mol. Microbiol. 15, 795-802.
    • (1995) Mol. Microbiol. , vol.15 , pp. 795-802
    • Parker, C.1    Barnell, W.O.2    Snoep, J.L.3    Ingram, L.O.4    Conway, T.5
  • 24
    • 0028000790 scopus 로고
    • Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria
    • Titgemeyer, F., Reizer, J., Reizer, A., and Saier, M. H. (1994) Evolutionary relationships between sugar kinases and transcriptional repressors in bacteria, Microbiology 140, 2349-2354.
    • (1994) Microbiology , vol.140 , pp. 2349-2354
    • Titgemeyer, F.1    Reizer, J.2    Reizer, A.3    Saier, M.H.4
  • 25
    • 2542536523 scopus 로고    scopus 로고
    • Mutagenic PCR of protein-encoding genes of in vivo evolution
    • Matsumura, I., and Ellington, A. D. (2001) Mutagenic PCR of protein-encoding genes of in vivo evolution, Methods Mol. Biol. 182, 261-269.
    • (2001) Methods Mol. Biol. , vol.182 , pp. 261-269
    • Matsumura, I.1    Ellington, A.D.2
  • 27
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins, Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 28
    • 0025879707 scopus 로고
    • Expression of human brain hexokinase in Escherichia coli: Purification and characterization of the expressed enzyme
    • Liu, F., Dong, Q., Myers, A. M., and Fromm, H. J. (1991) Expression of human brain hexokinase in Escherichia coli: Purification and characterization of the expressed enzyme, Biochem. Biophys. Res. Commun. 177, 305-311.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 305-311
    • Liu, F.1    Dong, Q.2    Myers, A.M.3    Fromm, H.J.4
  • 29
    • 0015504296 scopus 로고
    • Identification and properties of an inducible mannokinase from Streptomyces violaceoruber
    • Sabater, B., Sebastian, J., and Asensio, C. (1972) Identification and properties of an inducible mannokinase from Streptomyces violaceoruber, Biochim. Biophys. Acta 284, 406-414.
    • (1972) Biochim. Biophys. Acta , vol.284 , pp. 406-414
    • Sabater, B.1    Sebastian, J.2    Asensio, C.3
  • 30
    • 0016761881 scopus 로고
    • Phosphorylation of D-glucose in Escherichia coli mutants defective in glucosephosphotransferase, mannosephosphotransferase, and glucokinase
    • Curtis, S. J., and 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
  • 33
    • 0036305943 scopus 로고    scopus 로고
    • Sequence and structure classification of kinases
    • Cheek, S., Zhang, H., and Grishin, N. V. (2002) Sequence and structure classification of kinases, J. Mol. Biol. 320, 855-881.
    • (2002) J. Mol. Biol. , vol.320 , pp. 855-881
    • Cheek, S.1    Zhang, H.2    Grishin, N.V.3
  • 34
    • 0032929297 scopus 로고    scopus 로고
    • Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli
    • Plumbridge, J., and Vimr, E. (1999) Convergent pathways for utilization of the amino sugars N-acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by Escherichia coli, J. Bacteriol. 181, 47-54.
    • (1999) J. Bacteriol. , vol.181 , pp. 47-54
    • Plumbridge, J.1    Vimr, E.2
  • 35
    • 0028279839 scopus 로고
    • Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic glutamic acid 165 is changed to aspartic acid
    • Joseph-McCarthy, D., Rost, L. E., Komives, E. A., and Petsko, G. A. (1994) Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic glutamic acid 165 is changed to aspartic acid, Biochemistry 33, 2824-2829.
    • (1994) Biochemistry , vol.33 , pp. 2824-2829
    • Joseph-McCarthy, D.1    Rost, L.E.2    Komives, E.A.3    Petsko, G.A.4
  • 36
    • 0028884130 scopus 로고
    • The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of the active site water molecules
    • Komives, E. A., Lougheed, J. C., Liu, K., Suglo, S., Zhang, Z., Petsko, G. A., and Ringe, D. (1995) The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of the active site water molecules, Biochemistry 34, 13612-13621.
    • (1995) Biochemistry , vol.34 , pp. 13612-13621
    • Komives, E.A.1    Lougheed, J.C.2    Liu, K.3    Suglo, S.4    Zhang, Z.5    Petsko, G.A.6    Ringe, D.7
  • 37
    • 0022971122 scopus 로고
    • Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate
    • Raines, R. T., Sutton, E. L., Straus, D. R., Gilbert, W., and Knowles, J. R. (1986) Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate, Biochemistry 25, 7142-7154.
    • (1986) Biochemistry , vol.25 , pp. 7142-7154
    • Raines, R.T.1    Sutton, E.L.2    Straus, D.R.3    Gilbert, W.4    Knowles, J.R.5
  • 39
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork, P., Sander, C., and Valencia, A. (1993) Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases, Protein Sci. 2, 31-40.
    • (1993) Protein Sci. , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 40
    • 0035078573 scopus 로고    scopus 로고
    • Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon
    • Ito, S., Fushinobu, S., Yoshioka, I., Koga, S., Matsuzawa, H., and Wakagi, T. (2001) Structural basis for the ADP-specificity of a novel glucokinase from a hyperthermophilic archaeon, Structure 9, 205-214.
    • (2001) Structure , vol.9 , pp. 205-214
    • Ito, S.1    Fushinobu, S.2    Yoshioka, I.3    Koga, S.4    Matsuzawa, H.5    Wakagi, T.6
  • 41
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • O'Brien, P. J., and Herschlag, D. (1999) Catalytic promiscuity and the evolution of new enzymatic activities, Chem. Biol. 6, R91-R105.
    • (1999) Chem. Biol. , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 42
    • 0038625074 scopus 로고    scopus 로고
    • Mimicking natural evolution in vitro: An N-acetylneuraminate lyase mutant with an increased dihydropicolinate synthase activity
    • Joerger, A. C., Mayer, A., and Fersht, A. R. (2003) Mimicking natural evolution in vitro: An N-acetylneuraminate lyase mutant with an increased dihydropicolinate synthase activity, Proc. Natl. Acad. Sci. U.S.A. 100, 5694-5699.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 5694-5699
    • Joerger, A.C.1    Mayer, A.2    Fersht, A.R.3
  • 43
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • Copley, S. D. (2003) Enzymes with extra talents: Moonlighting functions and catalytic promiscuity, Curr. Opin. Chem. Biol. 7, 265-272.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 265-272
    • Copley, S.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.