메뉴 건너뛰기




Volumn 8, Issue 5-6, 2008, Pages 471-483

Molecular modeling and docking studies of glutamate racemase in Vibrio vulnificus CMCP6

Author keywords

Docking; Glutamate racemase; Modeller; Vibrio vulnificus

Indexed keywords

AMINO ACID ISOMERASES; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; COMPUTER SIMULATION; CONSERVED SEQUENCE; ENZYME INHIBITORS; HYDROGEN BONDING; IMAGING, THREE-DIMENSIONAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY, PROTEIN; VIBRIO VULNIFICUS;

EID: 58149373923     PISSN: 13866338     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (9)

References (26)
  • 1
    • 0035018011 scopus 로고    scopus 로고
    • Formation of the glycan chains in the synthesis of bacterial peptidoglycan
    • van Heijenoort, J. (2001). Formation of the glycan chains in the synthesis of bacterial peptidoglycan. Glycobiology 11, 25R-36R.
    • (2001) Glycobiology , vol.11
    • van Heijenoort, J.1
  • 2
    • 0032039227 scopus 로고    scopus 로고
    • Assembly of the monomer unit of bacterial peptidoglycan
    • van Heijenoort, J. (1998). Assembly of the monomer unit of bacterial peptidoglycan. Cell. Mol. Life Sci. 54, 300-304.
    • (1998) Cell. Mol. Life Sci , vol.54 , pp. 300-304
    • van Heijenoort, J.1
  • 5
    • 0035967535 scopus 로고    scopus 로고
    • Active site residues of glutamate racemase
    • Glavas, S. and Tanner, M. E. (2001). Active site residues of glutamate racemase. Biochemistry 40, 6199-6204.
    • (2001) Biochemistry , vol.40 , pp. 6199-6204
    • Glavas, S.1    Tanner, M.E.2
  • 6
    • 15944429289 scopus 로고    scopus 로고
    • Molecular pathogenesis of Vibrio vulnificus
    • Gulig, P. A., Bourdage, K. L. and Starks, A. M. (2005). Molecular pathogenesis of Vibrio vulnificus. J. Microbiol. 43, 118-131.
    • (2005) J. Microbiol , vol.43 , pp. 118-131
    • Gulig, P.A.1    Bourdage, K.L.2    Starks, A.M.3
  • 7
    • 20844455738 scopus 로고    scopus 로고
    • Wound infections caused by Vibrio vulnificus and other marine bacteria
    • Oliver, J. D. (2005). Wound infections caused by Vibrio vulnificus and other marine bacteria. Epidemiol. Infect. 133, 383-391.
    • (2005) Epidemiol. Infect , vol.133 , pp. 383-391
    • Oliver, J.D.1
  • 8
  • 9
    • 0032936626 scopus 로고    scopus 로고
    • Pathogenesis of Vibrio vulnificus
    • Linkous, D. A. and Oliver, J. D. (1999). Pathogenesis of Vibrio vulnificus. FEMS Microbiol. Lett. 174, 207-214.
    • (1999) FEMS Microbiol. Lett , vol.174 , pp. 207-214
    • Linkous, D.A.1    Oliver, J.D.2
  • 10
    • 0034100450 scopus 로고    scopus 로고
    • Epidemiology and pathogenesis of Vibrio vulnificus
    • Strom, M. S. and Paranjpye, R. N. (2000). Epidemiology and pathogenesis of Vibrio vulnificus. Microbes Infect. 2, 177-188.
    • (2000) Microbes Infect , vol.2 , pp. 177-188
    • Strom, M.S.1    Paranjpye, R.N.2
  • 11
    • 0022006016 scopus 로고
    • Relation of capsular materials and colony opacity to virulence of Vibrio vulnificus
    • Yoshida, S., Ogawa, M. and Mizuguchi, Y. (1985). Relation of capsular materials and colony opacity to virulence of Vibrio vulnificus. Infect. Immun. 47, 446-451.
    • (1985) Infect. Immun , vol.47 , pp. 446-451
    • Yoshida, S.1    Ogawa, M.2    Mizuguchi, Y.3
  • 12
    • 0020615792 scopus 로고
    • Siderophore production by Vibrio vulnificus
    • Simpson, L. M. and Oliver J. D. (1983). Siderophore production by Vibrio vulnificus. Infect. Immun. 41, 644-649.
    • (1983) Infect. Immun , vol.41 , pp. 644-649
    • Simpson, L.M.1    Oliver, J.D.2
  • 14
    • 0023196767 scopus 로고
    • Inhibitory effect of capsular antigen of Vibrio vulnificus on bactericidal activity of human serum
    • Shinoda, S., Kobayashi, M., Yamada, H., Yoshida, S., Ogawa, M. and Mizuguchi, Y. (1987). Inhibitory effect of capsular antigen of Vibrio vulnificus on bactericidal activity of human serum. Microbiol. Immunol. 31, 393-401.
    • (1987) Microbiol. Immunol , vol.31 , pp. 393-401
    • Shinoda, S.1    Kobayashi, M.2    Yamada, H.3    Yoshida, S.4    Ogawa, M.5    Mizuguchi, Y.6
  • 15
    • 0037369796 scopus 로고    scopus 로고
    • Identification of genetic loci required for capsular expression in Vibrio vulnificus
    • Smith, A. B. and Siebeling, R. J. (2003). Identification of genetic loci required for capsular expression in Vibrio vulnificus. Infect. Immun. 71, 1091-1097.
    • (2003) Infect. Immun , vol.71 , pp. 1091-1097
    • Smith, A.B.1    Siebeling, R.J.2
  • 16
    • 0028263397 scopus 로고
    • The synthesis and stability of aziridino-glutamate, an irreversible inhibitor of glutamate racemase
    • Tanner,M. E. and Miao, S. (1994). The synthesis and stability of aziridino-glutamate, an irreversible inhibitor of glutamate racemase. Tetrahedron Lett. 35, 4073-4076.
    • (1994) Tetrahedron Lett , vol.35 , pp. 4073-4076
    • Tanner, M.E.1    Miao, S.2
  • 17
    • 0002679348 scopus 로고
    • Inactivation of glutamate racemase of Pediococcus pentosaceus with L-serine O-sulfate
    • Ashiuchi, M., Yoshimura, T., Esaki, N., Uneo, H. and Soda, K. (1993). Inactivation of glutamate racemase of Pediococcus pentosaceus with L-serine O-sulfate. Biosci. Biotechnol. Biochem. 57, 1978-1979.
    • (1993) Biosci. Biotechnol. Biochem , vol.57 , pp. 1978-1979
    • Ashiuchi, M.1    Yoshimura, T.2    Esaki, N.3    Uneo, H.4    Soda, K.5
  • 19
    • 0032915050 scopus 로고    scopus 로고
    • Structure and mechanism of glutamate racemase from Aquifex pyrophilus
    • Hwang, K. Y., Cho, C.-S., Kim, S. S., Sung, H.-C., Yu, Y. G. and Cho, Y. (1999). Structure and mechanism of glutamate racemase from Aquifex pyrophilus. Nat. Struct. Biol. 6, 422-426.
    • (1999) Nat. Struct. Biol , vol.6 , pp. 422-426
    • Hwang, K.Y.1    Cho, C.-S.2    Kim, S.S.3    Sung, H.-C.4    Yu, Y.G.5    Cho, Y.6
  • 22
    • 27644453362 scopus 로고    scopus 로고
    • Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery
    • Ruzheinikov, S. N., Taal, M. A., Sedelnikova, S. E., Baker, P. J. and Rice, D.W. (2005). Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery. Structure 13, 1707-1713.
    • (2005) Structure , vol.13 , pp. 1707-1713
    • Ruzheinikov, S.N.1    Taal, M.A.2    Sedelnikova, S.E.3    Baker, P.J.4    Rice, D.W.5
  • 23
    • 34447526743 scopus 로고    scopus 로고
    • Functional comparison of the two Bacillus anthracis glutamate racemases
    • Dodd, D., Reese, J. G., Louer, C. R., Ballard, J. D., Spies, M. A. and Blanke, S. R. (2007). Functional comparison of the two Bacillus anthracis glutamate racemases. J. Bacteriol. 189, 5265-5275.
    • (2007) J. Bacteriol , vol.189 , pp. 5265-5275
    • Dodd, D.1    Reese, J.G.2    Louer, C.R.3    Ballard, J.D.4    Spies, M.A.5    Blanke, S.R.6
  • 24
    • 0027299709 scopus 로고
    • Mechanism of the reaction catalyzed by glutamate racemase
    • Gallo, K. A., Tanner, M. E. and Knowles, J. R. (1993). Mechanism of the reaction catalyzed by glutamate racemase. Biochemistry 32, 3991-3997.
    • (1993) Biochemistry , vol.32 , pp. 3991-3997
    • Gallo, K.A.1    Tanner, M.E.2    Knowles, J.R.3
  • 25
    • 3342957245 scopus 로고    scopus 로고
    • Multiple substrate binding states and chiral recognition in cofactor-independent glutamate racemase: A molecular dynamics study
    • Möbitz, H. and Bruice, T. C. (2004). Multiple substrate binding states and chiral recognition in cofactor-independent glutamate racemase: A molecular dynamics study. Biochemistry 43, 9685-9694.
    • (2004) Biochemistry , vol.43 , pp. 9685-9694
    • Möbitz, H.1    Bruice, T.C.2
  • 26
    • 0033616629 scopus 로고    scopus 로고
    • Catalytic acid/base residues of glutamate racemase
    • Glavas, S. and Tanner, M. E. (1999). Catalytic acid/base residues of glutamate racemase. Biochemistry 38, 4106-4113.
    • (1999) Biochemistry , vol.38 , pp. 4106-4113
    • Glavas, S.1    Tanner, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.