메뉴 건너뛰기




Volumn 91, Issue 2, 2009, Pages 204-213

UDPglucose pyrophosphorylase from Xanthomonas spp. Characterization of the enzyme kinetics, structure and inactivation related to oligomeric dissociation

Author keywords

Oligomeric dissociation; Polysaccharides; UDPglucose pyrophosphorylase; Xanthomonas

Indexed keywords

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; CLONING, MOLECULAR; CONSERVED SEQUENCE; DIMERIZATION; ESCHERICHIA COLI; GENE AMPLIFICATION; GENES, BACTERIAL; GENETIC VECTORS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PLASMIDS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; TRANSFORMATION, BACTERIAL; UTP-GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE; XANTHOMONAS;

EID: 58849117988     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.09.001     Document Type: Article
Times cited : (25)

References (44)
  • 1
    • 0028244580 scopus 로고
    • Overproduction and characterization of recombinant UDP-glucose pyrophosphorylase from Escherichia coli K-12
    • Hossain S.A., Tanizawa K., Kazuta Y., and Fukui T. Overproduction and characterization of recombinant UDP-glucose pyrophosphorylase from Escherichia coli K-12. J. Biochem. (Tokyo) 115 (1994) 965-972
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 965-972
    • Hossain, S.A.1    Tanizawa, K.2    Kazuta, Y.3    Fukui, T.4
  • 2
    • 0029920614 scopus 로고    scopus 로고
    • The Leloir pathway: a mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose
    • Frey P.A. The Leloir pathway: a mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose. FASEB J. 10 (1996) 461-470
    • (1996) FASEB J. , vol.10 , pp. 461-470
    • Frey, P.A.1
  • 3
    • 0242498430 scopus 로고    scopus 로고
    • Structure and function of enzymes of the Leloir pathway for galactose metabolism
    • Holden H.M., Rayment I., and Thoden J.B. Structure and function of enzymes of the Leloir pathway for galactose metabolism. J. Biol. Chem. 278 (2003) 43885-43888
    • (2003) J. Biol. Chem. , vol.278 , pp. 43885-43888
    • Holden, H.M.1    Rayment, I.2    Thoden, J.B.3
  • 4
    • 0031744365 scopus 로고    scopus 로고
    • Characterization of the galU gene of Streptococcus pneumoniae encoding a uridine diphosphoglucose pyrophosphorylase: a gene essential for capsular polysaccharide biosynthesis
    • Mollerach M., Lopez R., and Garcia E. Characterization of the galU gene of Streptococcus pneumoniae encoding a uridine diphosphoglucose pyrophosphorylase: a gene essential for capsular polysaccharide biosynthesis. J. Exp. Med. 188 (1998) 2047-2056
    • (1998) J. Exp. Med. , vol.188 , pp. 2047-2056
    • Mollerach, M.1    Lopez, R.2    Garcia, E.3
  • 5
    • 0028181852 scopus 로고
    • UTP: alpha-d-glucose-1-phosphate uridylyltransferase of Escherichia coli: isolation and DNA sequence of the galU gene and purification of the enzyme
    • Weissborn A.C., Liu Q., Rumley M.K., and Kennedy E.P. UTP: alpha-d-glucose-1-phosphate uridylyltransferase of Escherichia coli: isolation and DNA sequence of the galU gene and purification of the enzyme. J. Bacteriol. 176 (1994) 2611-2618
    • (1994) J. Bacteriol. , vol.176 , pp. 2611-2618
    • Weissborn, A.C.1    Liu, Q.2    Rumley, M.K.3    Kennedy, E.P.4
  • 6
    • 0034736572 scopus 로고    scopus 로고
    • The galU gene of Streptococcus pneumoniae that codes for a UDP-glucose pyrophosphorylase is highly polymorphic and suitable for molecular typing and phylogenetic studies
    • Mollerach M., and Garcia E. The galU gene of Streptococcus pneumoniae that codes for a UDP-glucose pyrophosphorylase is highly polymorphic and suitable for molecular typing and phylogenetic studies. Gene 260 (2000) 77-86
    • (2000) Gene , vol.260 , pp. 77-86
    • Mollerach, M.1    Garcia, E.2
  • 7
    • 33847298203 scopus 로고    scopus 로고
    • The molecular architecture of glucose-1-phosphate uridylyltransferase
    • Thoden J.B., and Holden H.M. The molecular architecture of glucose-1-phosphate uridylyltransferase. Protein Sci. 16 (2007) 432-440
    • (2007) Protein Sci. , vol.16 , pp. 432-440
    • Thoden, J.B.1    Holden, H.M.2
  • 8
    • 26444529002 scopus 로고    scopus 로고
    • Biochemical characterization of the pneumococcal glucose 1-phosphate uridylyltransferase (GalU) essential for capsule biosynthesis
    • Bonofiglio L., Garcia E., and Mollerach M. Biochemical characterization of the pneumococcal glucose 1-phosphate uridylyltransferase (GalU) essential for capsule biosynthesis. Curr. Microbiol. 51 (2005) 217-221
    • (2005) Curr. Microbiol. , vol.51 , pp. 217-221
    • Bonofiglio, L.1    Garcia, E.2    Mollerach, M.3
  • 9
    • 0029882684 scopus 로고    scopus 로고
    • Virulence and outer membrane properties of a galU mutant of Klebsiella pneumoniae CG43
    • Chang H.Y., Lee J.H., Deng W.L., Fu T.F., and Peng H.L. Virulence and outer membrane properties of a galU mutant of Klebsiella pneumoniae CG43. Microb. Pathog. 20 (1996) 255-261
    • (1996) Microb. Pathog. , vol.20 , pp. 255-261
    • Chang, H.Y.1    Lee, J.H.2    Deng, W.L.3    Fu, T.F.4    Peng, H.L.5
  • 10
    • 0037035424 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa galU is required for a complete lipopolysaccharide core and repairs a secondary mutation in a PA103 (serogroup O11) wbpM mutant
    • Dean C.R., and Goldberg J.B. Pseudomonas aeruginosa galU is required for a complete lipopolysaccharide core and repairs a secondary mutation in a PA103 (serogroup O11) wbpM mutant. FEMS Microbiol. Lett. 210 (2002) 277-283
    • (2002) FEMS Microbiol. Lett. , vol.210 , pp. 277-283
    • Dean, C.R.1    Goldberg, J.B.2
  • 11
    • 0028861531 scopus 로고
    • A virulence of rough mutants of Shigella flexneri: requirement of O antigen for correct unipolar localization of IcsA in the bacterial outer membrane
    • Sandlin R.C., Lampel K.A., Keasler S.P., Goldberg M.B., Stolzer A.L., and Maurelli A.T. A virulence of rough mutants of Shigella flexneri: requirement of O antigen for correct unipolar localization of IcsA in the bacterial outer membrane. Infect. Immun. 63 (1995) 229-237
    • (1995) Infect. Immun. , vol.63 , pp. 229-237
    • Sandlin, R.C.1    Lampel, K.A.2    Keasler, S.P.3    Goldberg, M.B.4    Stolzer, A.L.5    Maurelli, A.T.6
  • 12
    • 0027404233 scopus 로고
    • Involvement of lipopolysaccharide in the secretion of Escherichia coli alpha-haemolysin and Erwinia chrysanthemi proteases
    • Wandersman C., and Letoffe S. Involvement of lipopolysaccharide in the secretion of Escherichia coli alpha-haemolysin and Erwinia chrysanthemi proteases. Mol. Microbiol. 7 (1993) 141-150
    • (1993) Mol. Microbiol. , vol.7 , pp. 141-150
    • Wandersman, C.1    Letoffe, S.2
  • 13
    • 23744492608 scopus 로고    scopus 로고
    • Proteins encoded by Sphingomonas elodea ATCC 31461 rmlA and ugpG genes, involved in gellan gum biosynthesis, exhibit both dTDP- and UDP-glucose pyrophosphorylase activities
    • Silva E., Marques A.R., Fialho A.M., Granja A.T., and Sa-Correia I. Proteins encoded by Sphingomonas elodea ATCC 31461 rmlA and ugpG genes, involved in gellan gum biosynthesis, exhibit both dTDP- and UDP-glucose pyrophosphorylase activities. Appl. Environ. Microbiol. 71 (2005) 4703-4712
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4703-4712
    • Silva, E.1    Marques, A.R.2    Fialho, A.M.3    Granja, A.T.4    Sa-Correia, I.5
  • 14
    • 0031688984 scopus 로고    scopus 로고
    • Xanthan gum biosynthesis and application: a biochemical/genetic perspective
    • Becker A., Katzen F., Puhler A., and Ielpi L. Xanthan gum biosynthesis and application: a biochemical/genetic perspective. Appl. Microbiol. Biotechnol. 50 (1998) 145-152
    • (1998) Appl. Microbiol. Biotechnol. , vol.50 , pp. 145-152
    • Becker, A.1    Katzen, F.2    Puhler, A.3    Ielpi, L.4
  • 15
    • 34547098011 scopus 로고    scopus 로고
    • Xanthan is not essential for pathogenicity in citrus canker but contributes to Xanthomonas epiphytic survival
    • Dunger G., Relling V.M., Tondo M.L., Barreras M., Ielpi L., Orellano E.G., and Ottado J. Xanthan is not essential for pathogenicity in citrus canker but contributes to Xanthomonas epiphytic survival. Arch. Microbiol. 188 (2007) 127-135
    • (2007) Arch. Microbiol. , vol.188 , pp. 127-135
    • Dunger, G.1    Relling, V.M.2    Tondo, M.L.3    Barreras, M.4    Ielpi, L.5    Orellano, E.G.6    Ottado, J.7
  • 16
    • 0035020788 scopus 로고    scopus 로고
    • Expression of the gum operon directing xanthan biosynthesis in Xanthomonas campestris and its regulation in planta
    • Vojnov A.A., Slater H., Daniels M.J., and Dow J.M. Expression of the gum operon directing xanthan biosynthesis in Xanthomonas campestris and its regulation in planta. Mol. Plant. Microbe Interact. 14 (2001) 768-774
    • (2001) Mol. Plant. Microbe Interact. , vol.14 , pp. 768-774
    • Vojnov, A.A.1    Slater, H.2    Daniels, M.J.3    Dow, J.M.4
  • 18
    • 0030600379 scopus 로고    scopus 로고
    • The gene encoding UDP-glucose pyrophosphorylase is required for the synthesis of xanthan gum in Xanthomonas campestris
    • Wei C.L., Lin N.T., Weng S.F., and Tseng Y.H. The gene encoding UDP-glucose pyrophosphorylase is required for the synthesis of xanthan gum in Xanthomonas campestris. Biochem. Biophys. Res. Commun. 226 (1996) 607-612
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 607-612
    • Wei, C.L.1    Lin, N.T.2    Weng, S.F.3    Tseng, Y.H.4
  • 19
    • 0025836976 scopus 로고
    • Location and cloning of the ketal pyruvate transferase gene of Xanthomonas campestris
    • Marzocca M.P., Harding N.E., Petroni E.A., Cleary J.M., and Ielpi L. Location and cloning of the ketal pyruvate transferase gene of Xanthomonas campestris. J. Bacteriol. 173 (1991) 7519-7524
    • (1991) J. Bacteriol. , vol.173 , pp. 7519-7524
    • Marzocca, M.P.1    Harding, N.E.2    Petroni, E.A.3    Cleary, J.M.4    Ielpi, L.5
  • 22
    • 0000500140 scopus 로고
    • Subunit structure of spinach leaf ADPglucose pyrophosphorylase
    • Morell M.K., Bloom M., Knowles V., and Preiss J. Subunit structure of spinach leaf ADPglucose pyrophosphorylase. Plant Physiol. 85 (1987) 182-187
    • (1987) Plant Physiol. , vol.85 , pp. 182-187
    • Morell, M.K.1    Bloom, M.2    Knowles, V.3    Preiss, J.4
  • 23
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0001522673 scopus 로고
    • Starch-gel electrophoresis - application to the classification of pituitary proteins and polypeptides
    • Ferguson K.A. Starch-gel electrophoresis - application to the classification of pituitary proteins and polypeptides. Metabolism 13 (1964) 985-1002
    • (1964) Metabolism , vol.13 , pp. 985-1002
    • Ferguson, K.A.1
  • 26
    • 0020485873 scopus 로고
    • N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkers
    • Staros J.V. N-hydroxysulfosuccinimide active esters: bis(N-hydroxysulfosuccinimide) esters of two dicarboxylic acids are hydrophilic, membrane-impermeant, protein cross-linkers. Biochemistry 21 (1982) 3950-3955
    • (1982) Biochemistry , vol.21 , pp. 3950-3955
    • Staros, J.V.1
  • 27
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 28
    • 0033810049 scopus 로고    scopus 로고
    • Modeling of loops in protein structures
    • Fiser A., Do R.K., and Sali A. Modeling of loops in protein structures. Protein Sci. 9 (2000) 1753-1773
    • (2000) Protein Sci. , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.2    Sali, A.3
  • 30
    • 0034567210 scopus 로고    scopus 로고
    • Comparative protein structure modeling. Introduction and practical examples with modeller
    • Sanchez R., and Sali A. Comparative protein structure modeling. Introduction and practical examples with modeller. Methods Mol. Biol. 143 (2000) 97-129
    • (2000) Methods Mol. Biol. , vol.143 , pp. 97-129
    • Sanchez, R.1    Sali, A.2
  • 32
    • 0014767988 scopus 로고
    • Unified theory for gel electrophoresis and gel filtration
    • Rodbard D., and Chrambach A. Unified theory for gel electrophoresis and gel filtration. Proc Natl Acad Sci USA 65 (1970) 970-977
    • (1970) Proc Natl Acad Sci USA , vol.65 , pp. 970-977
    • Rodbard, D.1    Chrambach, A.2
  • 33
    • 0015245228 scopus 로고
    • Polyacrylamide gel electrophoresis
    • Chrambach A., and Rodbard D. Polyacrylamide gel electrophoresis. Science 172 (1971) 440-451
    • (1971) Science , vol.172 , pp. 440-451
    • Chrambach, A.1    Rodbard, D.2
  • 34
    • 4243241375 scopus 로고
    • Deternation of co-factor dissociation constants from the kinetics of inhibition of enzymes
    • Mildvan A.S., and Leigh R.A. Deternation of co-factor dissociation constants from the kinetics of inhibition of enzymes. Biochim. Biophys. Acta 89 (1964) 393-397
    • (1964) Biochim. Biophys. Acta , vol.89 , pp. 393-397
    • Mildvan, A.S.1    Leigh, R.A.2
  • 35
    • 0020189337 scopus 로고
    • Dynamics and time-averaged chemical potential of proteins: importance in oligomer association
    • Xu G., and Weber G. Dynamics and time-averaged chemical potential of proteins: importance in oligomer association. Proc Natl Acad Sci USA 79 (1982) 5268-5271
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5268-5271
    • Xu, G.1    Weber, G.2
  • 36
    • 34250856427 scopus 로고    scopus 로고
    • Active site geometry of glucose-1-phosphate uridylyltransferase
    • Thoden J.B., and Holden H.M. Active site geometry of glucose-1-phosphate uridylyltransferase. Protein Sci. 16 (2007) 1379-1388
    • (2007) Protein Sci. , vol.16 , pp. 1379-1388
    • Thoden, J.B.1    Holden, H.M.2
  • 37
    • 34250343820 scopus 로고    scopus 로고
    • The complex of Sphingomonas elodea ATCC 31461 glucose-1-phosphate uridylyltransferase with glucose-1-phosphate reveals a novel quaternary structure, unique among nucleoside diphosphate-sugar pyrophosphorylase members
    • Aragao D., Fialho A.M., Marques A.R., Mitchell E.P., Sa-Correia I., and Frazao C. The complex of Sphingomonas elodea ATCC 31461 glucose-1-phosphate uridylyltransferase with glucose-1-phosphate reveals a novel quaternary structure, unique among nucleoside diphosphate-sugar pyrophosphorylase members. J. Bacteriol. 189 (2007) 4520-4528
    • (2007) J. Bacteriol. , vol.189 , pp. 4520-4528
    • Aragao, D.1    Fialho, A.M.2    Marques, A.R.3    Mitchell, E.P.4    Sa-Correia, I.5    Frazao, C.6
  • 40
    • 33745216038 scopus 로고    scopus 로고
    • Molecular cloning of the Leishmania major UDP-glucose pyrophosphorylase, functional characterization, and ligand binding analyses using NMR spectroscopy
    • Lamerz A.C., Haselhorst T., Bergfeld A.K., von Itzstein M., and Gerardy-Schahn R. Molecular cloning of the Leishmania major UDP-glucose pyrophosphorylase, functional characterization, and ligand binding analyses using NMR spectroscopy. J. Biol. Chem. 281 (2006) 16,314-16,322
    • (2006) J. Biol. Chem. , vol.281
    • Lamerz, A.C.1    Haselhorst, T.2    Bergfeld, A.K.3    von Itzstein, M.4    Gerardy-Schahn, R.5
  • 42
    • 0036797918 scopus 로고    scopus 로고
    • Oligomerization status, with the monomer as active species, defines catalytic efficiency of UDP-glucose pyrophosphorylase
    • Martz F., Wilczynska M., and Kleczkowski L.A. Oligomerization status, with the monomer as active species, defines catalytic efficiency of UDP-glucose pyrophosphorylase. Biochem. J. 367 (2002) 295-300
    • (2002) Biochem. J. , vol.367 , pp. 295-300
    • Martz, F.1    Wilczynska, M.2    Kleczkowski, L.A.3
  • 44
    • 28344436830 scopus 로고    scopus 로고
    • Factors affecting oligomerization status of UDP-glucose pyrophosphorylase
    • Kleczkowski L.A., Martz F., and Wilczynska M. Factors affecting oligomerization status of UDP-glucose pyrophosphorylase. Phytochemistry 66 (2005) 2815-2821
    • (2005) Phytochemistry , vol.66 , pp. 2815-2821
    • Kleczkowski, L.A.1    Martz, F.2    Wilczynska, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.