메뉴 건너뛰기




Volumn 193, Issue 19, 2011, Pages 5393-5399

Characterization of a glucosamine/glucosaminide N-acetyltransferase of Clostridium acetobutylicum

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A; ACYLTRANSFERASE; BACTERIAL ENZYME; CHITOSAN DERIVATIVE; GLUCOSAMINE; GLUCOSAMINE GLUCOSAMINIDE N ACETYLTRANSFERASE; N ACETYLGLUCOSAMINE; PEPTIDOGLYCAN; UNCLASSIFIED DRUG;

EID: 80053584668     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05519-11     Document Type: Article
Times cited : (25)

References (34)
  • 1
    • 0015212189 scopus 로고
    • Enzymatic deacetylation of N-acetylglucosamine residues in peptidoglycan from Bacillus cereus cell walls
    • Araki, Y., S. Fukuoka, S. Oba, and E. Ito. 1971. Enzymatic deacetylation of N-acetylglucosamine residues in peptidoglycan from Bacillus cereus cell walls. Biochem. Biophys. Res. Commun. 45:751-758.
    • (1971) Biochem. Biophys. Res. Commun. , vol.45 , pp. 751-758
    • Araki, Y.1    Fukuoka, S.2    Oba, S.3    Ito, E.4
  • 2
    • 0015231851 scopus 로고
    • Occurrence of non-N-substituted glucosamine residues in lysozyme-resistant peptidoglycan from Bacillus cereus cell walls
    • Araki, Y., T. Nakatani, H. Hayashi, and E. Ito. 1971. Occurrence of non-N-substituted glucosamine residues in lysozyme-resistant peptidoglycan from Bacillus cereus cell walls. Biochem. Biophys. Res. Commun. 42:691-697.
    • (1971) Biochem. Biophys. Res. Commun. , vol.42 , pp. 691-697
    • Araki, Y.1    Nakatani, T.2    Hayashi, H.3    Ito, E.4
  • 3
    • 0032985757 scopus 로고    scopus 로고
    • Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation
    • Atrih, A., G. Bacher, G. Allmaier, M. P. Williamson, and S. J. Foster. 1999. Analysis of peptidoglycan structure from vegetative cells of Bacillus subtilis 168 and role of PBP 5 in peptidoglycan maturation. J. Bacteriol. 181:3956-3966.
    • (1999) J. Bacteriol. , vol.181 , pp. 3956-3966
    • Atrih, A.1    Bacher, G.2    Allmaier, G.3    Williamson, M.P.4    Foster, S.J.5
  • 4
    • 0022195520 scopus 로고
    • Acetyl coenzyme A: α-glucosaminide N-acetyltransferase: evidence for a transmembrane acetylation mechanism
    • Bame, K. J., and L. H. Rome. 1985. Acetyl coenzyme A:α-glucosaminide N-acetyltransferase: evidence for a transmembrane acetylation mechanism. J. Biol. Chem. 260:11293-11299.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11293-11299
    • Bame, K.J.1    Rome, L.H.2
  • 5
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani, G. 1951. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62:293-300.
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 6
    • 0003191832 scopus 로고
    • BRL pUC host: Escherichia coli DH5α competent cells
    • Bethesda Research Laboratories
    • Bethesda Research Laboratories. 1986. BRL pUC host: Escherichia coli DH5α competent cells. Focus 8:9.
    • (1986) Focus , vol.8 , pp. 9
  • 7
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • Blattner, F. R., et al. 1997. The complete genome sequence of Escherichia coli K-12. Science 277:1453-1462.
    • (1997) Science , vol.277 , pp. 1453-1462
    • Blattner, F.R.1
  • 8
    • 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
  • 9
    • 70449459830 scopus 로고
    • The acetylation of D-glucosamine by pigeon liver extracts
    • Chou, T. C., and M. Soodak. 1952. The acetylation of D-glucosamine by pigeon liver extracts. J. Biol. Chem. 196:105-109.
    • (1952) J. Biol. Chem. , vol.196 , pp. 105-109
    • Chou, T.C.1    Soodak, M.2
  • 10
    • 0026591303 scopus 로고
    • Purification and characterization of an extracellular muramidase of Clostridium acetobutylicum ATCC 824 that acts on non-N-acetylated peptidoglycan
    • Croux, C., B. Canard, G. Goma, and P. Soucaille. 1992. Purification and characterization of an extracellular muramidase of Clostridium acetobutylicum ATCC 824 that acts on non-N-acetylated peptidoglycan. Appl. Environ. Microbiol. 58:1075-1081.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 1075-1081
    • Croux, C.1    Canard, B.2    Goma, G.3    Soucaille, P.4
  • 12
    • 0015579786 scopus 로고
    • Occurrence of glucosamine residues with free amino groups in cell wall peptidoglycan from bacilli as a factor responsible for resistance to lysozyme
    • Hayashi, H., Y. Araki, and E. Ito. 1973. Occurrence of glucosamine residues with free amino groups in cell wall peptidoglycan from bacilli as a factor responsible for resistance to lysozyme. J. Bacteriol. 113:592-598.
    • (1973) J. Bacteriol. , vol.113 , pp. 592-598
    • Hayashi, H.1    Araki, Y.2    Ito, E.3
  • 13
    • 24044450244 scopus 로고    scopus 로고
    • Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase"
    • Jaeger, T., M. Arsic, and C. Mayer. 2005. Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase." J. Biol. Chem. 280: 30100-30106.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30100-30106
    • Jaeger, T.1    Arsic, M.2    Mayer, C.3
  • 14
    • 0030814693 scopus 로고    scopus 로고
    • Thermoanaerobacter mathranii sp. nov., an ethanol-producing, extremely thermophilic anaerobic bacterium from a hot spring in Iceland
    • Larsen, L., P. Nielsen, and B. K. Ahring. 1997. Thermoanaerobacter mathranii sp. nov., an ethanol-producing, extremely thermophilic anaerobic bacterium from a hot spring in Iceland. Arch. Microbiol. 168:114-119.
    • (1997) Arch. Microbiol. , vol.168 , pp. 114-119
    • Larsen, L.1    Nielsen, P.2    Ahring, B.K.3
  • 15
    • 77955141315 scopus 로고    scopus 로고
    • Development of flow cytometry technique for detection of thinning of peptidoglycan layer as a result of solvent production by Clostridium pasteurianum
    • Linhová, M., et al. 2010. Development of flow cytometry technique for detection of thinning of peptidoglycan layer as a result of solvent production by Clostridium pasteurianum. Folia Microbiol. 55:340-344.
    • (2010) Folia Microbiol , vol.55 , pp. 340-344
    • Linhová, M.1
  • 16
    • 77953985367 scopus 로고    scopus 로고
    • Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by β-N-acetylglucosaminidase and N-acetylmuramyl-Lalanine amidase
    • Litzinger, S., et al. 2010. Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by β-N-acetylglucosaminidase and N-acetylmuramyl-Lalanine amidase. J. Bacteriol. 192:3132-3143.
    • (2010) J. Bacteriol. , vol.192 , pp. 3132-3143
    • Litzinger, S.1
  • 17
    • 78149234937 scopus 로고    scopus 로고
    • Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism
    • Litzinger, S., et al. 2010. Structural and kinetic analysis of Bacillus subtilis N-acetylglucosaminidase reveals a unique Asp-His dyad mechanism. J. Biol. Chem. 285:35675-35684.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35675-35684
    • Litzinger, S.1
  • 18
    • 0028989710 scopus 로고
    • Human acetylcoenzyme A: α-glucosaminide N-acetyltransferase: kinetic characterization and mechanistic interpretation
    • Meikle, P. J., A. M. Whittle, and J. J. Hopwood. 1995. Human acetylcoenzyme A:α-glucosaminide N-acetyltransferase: kinetic characterization and mechanistic interpretation. Biochem. J. 308:327-333.
    • (1995) Biochem. J. , vol.308 , pp. 327-333
    • Meikle, P.J.1    Whittle, A.M.2    Hopwood, J.J.3
  • 19
    • 0020181071 scopus 로고
    • Identification of 2-amino-2-deoxyglucose residues in the peptidoglucan of Streptococcus pneumoniae
    • Ohno, N., T. Yadomae, and T. Miyazaki. 1982. Identification of 2-amino-2-deoxyglucose residues in the peptidoglucan of Streptococcus pneumoniae. Carbohydr. Res. 107:152-155.
    • (1982) Carbohydr. Res. , vol.107 , pp. 152-155
    • Ohno, N.1    Yadomae, T.2    Miyazaki, T.3
  • 20
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan)
    • Park, J. T., and T. Uehara. 2008. How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol. Mol. Biol. Rev. 72:211-227.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 211-227
    • Park, J.T.1    Uehara, T.2
  • 21
    • 0028026211 scopus 로고
    • Membrane-bound glucosamine acetyltransferase in coleoptile segments of Avena sativa
    • Piro, G., M. Buffo, and G. Dalessandro. 1994. Membrane-bound glucosamine acetyltransferase in coleoptile segments of Avena sativa. Physiol. Plant 90:181-186.
    • (1994) Physiol. Plant , vol.90 , pp. 181-186
    • Piro, G.1    Buffo, M.2    Dalessandro, G.3
  • 22
    • 80053584469 scopus 로고    scopus 로고
    • Characterization of an N-acetylmuramic acid/N-acetylglucosamine kinase of Clostridium acetobutylicum
    • Reith, J., A. Berking, and C. Mayer. 2011. Characterization of an N-acetylmuramic acid/N-acetylglucosamine kinase of Clostridium acetobutylicum J. Bacteriol. 193:5386-5392.
    • (2011) J. Bacteriol. , vol.193 , pp. 5386-5392
    • Reith, J.1    Berking, A.2    Mayer, C.3
  • 23
    • 79960663578 scopus 로고    scopus 로고
    • Peptidoglycan turnover and recycling in Gram-positive bacteria
    • [Epub ahead of print.]
    • Reith, J., and C. Mayer. 2011. Peptidoglycan turnover and recycling in Gram-positive bacteria. Appl. Microbiol. Biotechnol. [Epub ahead of print.]
    • (2011) Appl. Microbiol. Biotechnol.
    • Reith, J.1    Mayer, C.2
  • 24
    • 0018416496 scopus 로고
    • Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid): a reexamination
    • Riddles, P. W., R. L. Blakeley, and B. Zerner. 1979. Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid): a reexamination. Anal. Biochem. 94: 75-81.
    • (1979) Anal. Biochem. , vol.94 , pp. 75-81
    • Riddles, P.W.1    Blakeley, R.L.2    Zerner, B.3
  • 25
    • 0020041978 scopus 로고
    • Peptidoglycan of Rhodopseudomonas viridis: partial lack of N-acetyl substitution of glucosamine
    • Schmelzer, E., J. Weckesser, R. Warth, and H. Mayer. 1982. Peptidoglycan of Rhodopseudomonas viridis: partial lack of N-acetyl substitution of glucosamine. J. Bacteriol. 149:151-155.
    • (1982) J. Bacteriol. , vol.149 , pp. 151-155
    • Schmelzer, E.1    Weckesser, J.2    Warth, R.3    Mayer, H.4
  • 26
    • 0033617146 scopus 로고    scopus 로고
    • A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein
    • Spiess, C., A. Beil, and M. Ehrmann. 1999. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-347.
    • (1999) Cell , vol.97 , pp. 339-347
    • Spiess, C.1    Beil, A.2    Ehrmann, M.3
  • 27
    • 34547613915 scopus 로고    scopus 로고
    • An anhydro-N-acetylmuramyl-L-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coli
    • Uehara, T., and J. T. Park. 2007. An anhydro-N-acetylmuramyl-L-alanine amidase with broad specificity tethered to the outer membrane of Escherichia coli. J. Bacteriol. 189:5634-5641.
    • (2007) J. Bacteriol. , vol.189 , pp. 5634-5641
    • Uehara, T.1    Park, J.T.2
  • 28
    • 9744255506 scopus 로고    scopus 로고
    • Structure and functions of the GNAT superfamily of acetyltransferases
    • Vetting, M. W., et al. 2005. Structure and functions of the GNAT superfamily of acetyltransferases. Arch. Biochem. Biophys. 433:212-226.
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 212-226
    • Vetting, M.W.1
  • 29
    • 39149102149 scopus 로고    scopus 로고
    • Structural variation in the glycan strands of bacterial peptidoglycan
    • Vollmer, W. 2008. Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol. Rev. 32:287-306.
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 287-306
    • Vollmer, W.1
  • 31
    • 0034617218 scopus 로고    scopus 로고
    • The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae
    • Vollmer, W., and A. Tomasz. 2000. The pgdA gene encodes for a peptidoglycan N-acetylglucosamine deacetylase in Streptococcus pneumoniae. J. Biol. Chem. 275:20496-20501.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20496-20501
    • Vollmer, W.1    Tomasz, A.2
  • 32
    • 0014251825 scopus 로고
    • Control of amino sugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars
    • White, R. J. 1968. Control of amino sugar metabolism in Escherichia coli and isolation of mutants unable to degrade amino sugars. Biochem. J. 106:847-858.
    • (1968) Biochem. J. , vol.106 , pp. 847-858
    • White, R.J.1
  • 33
    • 0014144186 scopus 로고
    • The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli
    • White, R. J., and C. A. Pasternak. 1967. The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli. Biochem. J. 105:121-125.
    • (1967) Biochem. J. , vol.105 , pp. 121-125
    • White, R.J.1    Pasternak, C.A.2
  • 34
    • 0034884397 scopus 로고    scopus 로고
    • Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China
    • Xue, Y., Y. Xu, Y. Liu, Y. Ma, and P. Zhou. 2001. Thermoanaerobacter tengcongensis sp. nov., a novel anaerobic, saccharolytic, thermophilic bacterium isolated from a hot spring in Tengcong, China. Int. J. Syst. Evol. Microbiol. 51:1335-1341.
    • (2001) Int. J. Syst. Evol. Microbiol. , vol.51 , pp. 1335-1341
    • Xue, Y.1    Xu, Y.2    Liu, Y.3    Ma, Y.4    Zhou, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.