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Volumn 10, Issue 2, 2010, Pages 66-75

Structural and functional features of UDP-N-acetylenolpyruvylglucosamine reductase of Mycobacterium tuberculosis H37Rv

Author keywords

Bacterial cell wall; Denaturation; Flavin adenine dinucleotide (FAD); Peptidoglycan biosynthesis; UDP N acetylenolpyruvylglucosamine reductase (MurB)

Indexed keywords

BACTERIAL ENZYME; DIVALENT CATION; GUANIDINE; PEPTIDOGLYCAN; UDP N ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE; UNCLASSIFIED DRUG; UREA;

EID: 84865362877     PISSN: 09738363     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (1)

References (31)
  • 1
    • 0035916228 scopus 로고    scopus 로고
    • Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme
    • Ahmed A, Akhtar MS, et al. (2001) Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme. Biochemistry, 40(7): 1945-1955.
    • (2001) Biochemistry , vol.40 , Issue.7 , pp. 1945-1955
    • Ahmed, A.1    Akhtar, M.S.2
  • 2
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade MA, Chacon P, et al. (1993) Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng., 6(4): 383-390.
    • (1993) Protein Eng , vol.6 , Issue.4 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2
  • 3
    • 67649565474 scopus 로고    scopus 로고
    • In silico structural characterization of Mycobacterium tuberculosis H37Rv UDP-W- acetylmuramate dehydrogenase
    • Babajan B, Anuradha CM, et al. (2009) In silico structural characterization of Mycobacterium tuberculosis H37Rv UDP-W- acetylmuramate dehydrogenase. Int. J. Integ. Biol., 6: 12-16.
    • (2009) Int. J. Integ. Biol , vol.6 , pp. 12-16
    • Babajan, B.1    Anuradha, C.M.2
  • 4
    • 39149083088 scopus 로고    scopus 로고
    • Cytoplasmic steps of peptidoglycan biosynthesis
    • Barreteau H, Kovac A, et al. (2008) Cytoplasmic steps of peptidoglycan biosynthesis. FEMSMicrobiol. Rev., 32(2): 168-207.
    • (2008) FEMSMicrobiol. Rev , vol.32 , Issue.2 , pp. 168-207
    • Barreteau, H.1    Kovac, A.2
  • 5
    • 0026670154 scopus 로고
    • Molecular relaxation spectroscopy of flavin adenine dinucleotide in wild type and mutant lipoamide dehydrogenase from Azotobacter vinelandii
    • Bastiaens PI, van Hoek A, et al. (1992) Molecular relaxation spectroscopy of flavin adenine dinucleotide in wild type and mutant lipoamide dehydrogenase from Azotobacter vinelandii. Biochemistry, 31(31): 7061-7068.
    • (1992) Biochemistry , vol.31 , Issue.31 , pp. 7061-7068
    • Bastiaens, P.I.1    van Hoek, A.2
  • 6
    • 0029056202 scopus 로고
    • An enzyme-substrate complex involved in bacterial cell wall biosynthesis
    • Benson TE, Filman DJ, et al. (1995) An enzyme-substrate complex involved in bacterial cell wall biosynthesis. Nat. Struct. Biol., 2(8): 644-653.
    • (1995) Nat. Struct. Biol , vol.2 , Issue.8 , pp. 644-653
    • Benson, T.E.1    Filman, D.J.2
  • 7
    • 0035957048 scopus 로고    scopus 로고
    • A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-W- Acetylenolpyruvylglucosamine reductase (MurB)
    • Benson TE, Harris MS, et al. (2001) A structural variation for MurB: X-ray crystal structure of Staphylococcus aureus UDP-W- Acetylenolpyruvylglucosamine reductase (MurB). Biochemistry, 40(8): 2340-2350.
    • (2001) Biochemistry , vol.40 , Issue.8 , pp. 2340-2350
    • Benson, T.E.1    Harris, M.S.2
  • 8
    • 0027512265 scopus 로고
    • Overexpression, purification, and mechanistic study of UDP-N-acetylenolpymvylglucosamine reductase
    • Benson TE, Marquardt JL, et al. (1993) Overexpression, purification, and mechanistic study of UDP-N-acetylenolpymvylglucosamine reductase. Biochemistry, 32(8): 2024-2030.
    • (1993) Biochemistry , vol.32 , Issue.8 , pp. 2024-2030
    • Benson, T.E.1    Marquardt, J.L.2
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (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
  • 10
    • 0015522150 scopus 로고
    • Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion
    • Chen YH, Yang JT, et al. (1972) Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry, 11(22): 4120-4131.
    • (1972) Biochemistry , vol.11 , Issue.22 , pp. 4120-4131
    • Chen, Y.H.1    Yang, J.T.2
  • 11
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole ST, Brosch R, et al. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature, 393(6685): 537-544.
    • (1998) Nature , vol.393 , Issue.6685 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2
  • 12
    • 0026559854 scopus 로고
    • Drug-resistant TB may bring epidemic
    • Culliton BJ (1992) Drug-resistant TB may bring epidemic. Nature, 356(6369): 473.
    • (1992) Nature , vol.356 , Issue.6369 , pp. 473
    • Culliton, B.J.1
  • 13
    • 0029007512 scopus 로고
    • Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase
    • Dlialla AM, Yanchunas J Jr, et al. (1995) Steady-state kinetic mechanism of Escherichia coli UDP-N-acetylenolpyruvylglucosamine reductase. Biochemistry, 34(16): 5390-5402.
    • (1995) Biochemistry , vol.34 , Issue.16 , pp. 5390-5402
    • Dlialla, A.M.1    Yanchunas Jr., J.2
  • 14
    • 0037339206 scopus 로고    scopus 로고
    • Identification of novel inhibitors of Pseudomonas aeruginosa MurC enzyme derived from phage-displayed peptide libraries
    • ElZoeiby A, Sanschagrin F, et al. (2003) Identification of novel inhibitors of Pseudomonas aeruginosa MurC enzyme derived from phage-displayed peptide libraries. J. Antimicrob. Chemother., 51(3): 531-543.
    • (2003) J. Antimicrob. Chemother , vol.51 , Issue.3 , pp. 531-543
    • Elzoeiby, A.1    Sanschagrin, F.2
  • 15
    • 0036480755 scopus 로고    scopus 로고
    • The bacterial cell wall as a source of antibacterial targets
    • Green DW (2002) The bacterial cell wall as a source of antibacterial targets. Expert Opin. Ther. Targets, 6(1): 1-19.
    • (2002) Expert Opin. Ther. Targets , vol.6 , Issue.1 , pp. 1-19
    • Green, D.W.1
  • 16
    • 0037241238 scopus 로고    scopus 로고
    • Structure-based design approaches to cell wall biosynthesis inhibitors
    • Katz AH and Caufreld CE (2003) Structure-based design approaches to cell wall biosynthesis inhibitors. Curr. Pharm. Des., 9(11): 857-866.
    • (2003) Curr. Pharm. Des , vol.9 , Issue.11 , pp. 857-866
    • Katz, A.H.1    Caufreld, C.E.2
  • 17
    • 33846218732 scopus 로고    scopus 로고
    • Crystal stmcture of UDP-N- acetylenolpyruvyl- glucosamine reductase (MurB) from Thermits caldophilus
    • Kim MK, Cho MK, et al. (2007) Crystal stmcture of UDP-N- acetylenolpyruvyl- glucosamine reductase (MurB) from Thermits caldophilus. Proteins, 66(3): 751-754.
    • (2007) Proteins , vol.66 , Issue.3 , pp. 751-754
    • Kim, M.K.1    Cho, M.K.2
  • 19
    • 0036090929 scopus 로고    scopus 로고
    • Novel targets for the future development of antibacterial agents
    • McDevitt D, Payne DJ, et al. (2002) Novel targets for the future development of antibacterial agents. J. Appi. Microbiol., 92: 28S-34S.
    • (2002) J. Appi. Microbiol , vol.92
    • McDevitt, D.1    Payne, D.J.2
  • 20
    • 0020458828 scopus 로고
    • Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli
    • Mengin-Lecreulx D, Flouret B, et al. (1982) Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli. J. Bacteriol, 151(3): 1109-1117.
    • (1982) J. Bacteriol , vol.151 , Issue.3 , pp. 1109-1117
    • Mengin-Lecreulx, D.1    Flouret, B.2
  • 21
    • 0026823076 scopus 로고
    • Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N- acetylenolpyruvoylglucosamine reductase
    • Pucci MJ, Discotto LF, et al. (1992) Cloning and identification of the Escherichia coli murB DNA sequence, which encodes UDP-N- acetylenolpyruvoylglucosamine reductase. J. Bacteriol, 174(5): 1690-1693.
    • (1992) J. Bacteriol , vol.174 , Issue.5 , pp. 1690-1693
    • Pucci, M.J.1    Discotto, L.F.2
  • 22
    • 0028905536 scopus 로고
    • Expression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase
    • Reddy SG, Sacchettini JC, et al. (1995) Expression, purification, and characterization of Escherichia coli dihydrodipicolinate reductase. Biochemistry, 34(11): 3492-3501.
    • (1995) Biochemistry , vol.34 , Issue.11 , pp. 3492-3501
    • Reddy, S.G.1    Sacchettini, J.C.2
  • 23
    • 0028822324 scopus 로고
    • The Bacillus subtilis cell- division 135-137 degrees region contains an essential orf with significant similarity to murB and a dispensable sbp gene
    • Rowland SL, Errington J, et al. (1995) The Bacillus subtilis cell- division 135-137 degrees region contains an essential orf with significant similarity to murB and a dispensable sbp gene. Gene, 164(1): 113-116.
    • (1995) Gene , vol.164 , Issue.1 , pp. 113-116
    • Rowland, S.L.1    Errington, J.2
  • 25
    • 0036199409 scopus 로고    scopus 로고
    • Determination of ligand-MurB interactions by isothermal denaturation: Application as a secondary assay to complement high throughput screening
    • Sarver RW, Rogers JM, et al. (2002) Determination of ligand-MurB interactions by isothermal denaturation: application as a secondary assay to complement high throughput screening. J. Biomol. Screen., 7(1): 21-28
    • (2002) J. Biomol. Screen , vol.7 , Issue.1 , pp. 21-28
    • Sarver, R.W.1    Rogers, J.M.2
  • 26
    • 16444367720 scopus 로고    scopus 로고
    • Cloning and characterization of aspartate-beta-semialdehyde dehydrogenase from Mycobacterium tuberculosis H37Rv
    • Sliafiani S, Slianna P, et al. (2005) Cloning and characterization of aspartate-beta-semialdehyde dehydrogenase from Mycobacterium tuberculosis H37Rv. J. Àppi. Microbiol., 98(4): 832-838.
    • (2005) J. Àppi. Microbiol , vol.98 , Issue.4 , pp. 832-838
    • Sliafiani, S.1    Slianna, P.2
  • 27
    • 0035871278 scopus 로고    scopus 로고
    • Identification and characterization of UDP-N-acetylenolpymvylglucosamine reductase (MurB) from the Gram-positive pathogen Streptococcus pneumoniae
    • Sylvester DR, Alvarez E, et al. (2001) Identification and characterization of UDP-N-acetylenolpymvylglucosamine reductase (MurB) from the Gram-positive pathogen Streptococcus pneumoniae. Biochem. J., 355(Pt 2): 431-435.
    • (2001) Biochem. J , vol.355 , Issue.PART 2 , pp. 431-435
    • Sylvester, D.R.1    Alvarez, E.2
  • 28
    • 0015579084 scopus 로고
    • Studies on the molecular complex of flavins. IV. Activity and FAD-fluorescence change caused by the chemical modification of tryptophyl and tyrosyl residues in glucose oxidase
    • Tsuge H and Mitsuda H (1973) Studies on the molecular complex of flavins. IV. Activity and FAD-fluorescence change caused by the chemical modification of tryptophyl and tyrosyl residues in glucose oxidase. J. Biochem., 73(2): 199-206.
    • (1973) J. Biochem , vol.73 , Issue.2 , pp. 199-206
    • Tsuge, H.1    Mitsuda, H.2
  • 29
    • 0028825801 scopus 로고
    • Epidemiology of tuberculosis by DNA fingerprinting
    • Van Soolingen D and Hermans PW (1995) Epidemiology of tuberculosis by DNA fingerprinting. Eur. Respir. J., 8(Suppl. 20): 649-656.
    • (1995) Eur. Respir. J , vol.8 , Issue.SUPPL. 20 , pp. 649-656
    • van Soolingen, D.1    Hermans, P.W.2
  • 30
    • 39149110299 scopus 로고    scopus 로고
    • Peptidoglycan structure and architecture
    • Vollmer W, Blanot D, et al (2008) Peptidoglycan structure and architecture. FEMS Microbiol. Rev. 32(2): 149-167.
    • (2008) FEMS Microbiol. Rev. , vol.32 , Issue.2 , pp. 149-167
    • Vollmer, W.1    Blanot, D.2
  • 31
    • 54949118875 scopus 로고    scopus 로고
    • World Health Organization
    • World Health Organization (2008) Tuberculosis. Fact sheet 104. http://www.who.int/tb/publications/2008/factsheet_april08.pdf.
    • (2008) Tuberculosis. Fact Sheet 104


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.