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Volumn 17, Issue 2, 2009, Pages 303-313

Structural Basis of Murein Peptide Specificity of a γ-D-Glutamyl-L-Diamino Acid Endopeptidase

(53)  Xu, Qingping a,b   Sudek, Sebastian a,c   McMullan, Daniel a,d   Miller, Mitchell D a,b   Geierstanger, Bernhard d   Jones, David H d   Krishna, S Sri a,e,f   Spraggon, Glen a,d   Bursalay, Badry d   Abdubek, Polat a,d   Acosta, Claire a,d   Ambing, Eileen a,d   Astakhova, Tamara a,e   Axelrod, Herbert L a,b   Carlton, Dennis a,c   Caruthers, Jonathan a,b   Chiu, Hsiu Ju a,b   Clayton, Thomas a,c   Deller, Marc C a,c   Duan, Lian a,e   more..


Author keywords

PROTEINS

Indexed keywords

ALANINE; GAMMA DEXTRO GLUTAMYLDIAMINO ACID ENDOPEPTIDASE; PAPAIN; PEPTIDOGLYCAN; PROTEIN P60; PROTEIN SH3; PROTEINASE; UNCLASSIFIED DRUG;

EID: 59649104674     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.12.008     Document Type: Article
Times cited : (62)

References (56)
  • 1
    • 18244415313 scopus 로고    scopus 로고
    • Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes
    • Anantharaman V., and Aravind L. Evolutionary history, structural features and biochemical diversity of the NlpC/P60 superfamily of enzymes. Genome Biol. 4 (2003) R11
    • (2003) Genome Biol. , vol.4
    • Anantharaman, V.1    Aravind, L.2
  • 2
    • 0034930561 scopus 로고    scopus 로고
    • Evolutionary lines of cysteine peptidases
    • Barrett A.J., and Rawlings N.D. Evolutionary lines of cysteine peptidases. Biol. Chem. 382 (2001) 727-733
    • (2001) Biol. Chem. , vol.382 , pp. 727-733
    • Barrett, A.J.1    Rawlings, N.D.2
  • 3
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman A., and Bycroft M. The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J. Mol. Biol. 299 (2000) 1113-1119
    • (2000) J. Mol. Biol. , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 4
    • 0038403691 scopus 로고    scopus 로고
    • The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases
    • Bateman A., and Rawlings N.D. The CHAP domain: a large family of amidases including GSP amidase and peptidoglycan hydrolases. Trends Biochem. Sci. 28 (2003) 234-237
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 234-237
    • Bateman, A.1    Rawlings, N.D.2
  • 6
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti P.J., and Storer A.C. Alignment/phylogeny of the papain superfamily of cysteine proteases. J. Mol. Biol. 246 (1995) 273-283
    • (1995) J. Mol. Biol. , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 7
    • 33645227952 scopus 로고    scopus 로고
    • Bacteriophage endolysins as a novel class of antibacterial agents
    • Borysowski J., Weber-Dabrowska B., and Gorski A. Bacteriophage endolysins as a novel class of antibacterial agents. Exp. Biol. Med. 231 (2006) 366-377
    • (2006) Exp. Biol. Med. , vol.231 , pp. 366-377
    • Borysowski, J.1    Weber-Dabrowska, B.2    Gorski, A.3
  • 8
    • 0026569755 scopus 로고
    • Purification and partial characterization of the γ-D-glutamyl-L-di-amino acid endopeptidase II from Bacillus sphaericus
    • Bourgogne T., Vacheron M.J., Guinand M., and Michel G. Purification and partial characterization of the γ-D-glutamyl-L-di-amino acid endopeptidase II from Bacillus sphaericus. Int. J. Biochem. 24 (1992) 471-476
    • (1992) Int. J. Biochem. , vol.24 , pp. 471-476
    • Bourgogne, T.1    Vacheron, M.J.2    Guinand, M.3    Michel, G.4
  • 9
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman H.A., Riese R.J., and Shi G.P. Emerging roles for cysteine proteases in human biology. Annu. Rev. Physiol. 59 (1997) 63-88
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 10
    • 3242886389 scopus 로고    scopus 로고
    • MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes
    • Davis I.W., Murray L.W., Richardson J.S., and Richardson D.C. MolProbity: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res. 32 (2004) W615-W619
    • (2004) Nucleic Acids Res. , vol.32
    • Davis, I.W.1    Murray, L.W.2    Richardson, J.S.3    Richardson, D.C.4
  • 11
    • 33746061682 scopus 로고    scopus 로고
    • The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain
    • Donovan D.M., Foster-Frey J., Dong S., Rousseau G.M., Moineau S., and Pritchard D.G. The cell lysis activity of the Streptococcus agalactiae bacteriophage B30 endolysin relies on the cysteine, histidine-dependent amidohydrolase/peptidase domain. Appl. Environ. Microbiol. 72 (2006) 5108-5112
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5108-5112
    • Donovan, D.M.1    Foster-Frey, J.2    Dong, S.3    Rousseau, G.M.4    Moineau, S.5    Pritchard, D.G.6
  • 12
    • 0035186065 scopus 로고    scopus 로고
    • A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA
    • Fernandez-Tornero C., Lopez R., Garcia E., Gimenez-Gallego G., and Romero A. A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA. Nat. Struct. Biol. 8 (2001) 1020-1024
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1020-1024
    • Fernandez-Tornero, C.1    Lopez, R.2    Garcia, E.3    Gimenez-Gallego, G.4    Romero, A.5
  • 13
    • 35448970693 scopus 로고    scopus 로고
    • Folds and activities of peptidoglycan amidases
    • Firczuk M., and Bochtler M. Folds and activities of peptidoglycan amidases. FEMS Microbiol. Rev. 31 (2007) 676-691
    • (2007) FEMS Microbiol. Rev. , vol.31 , pp. 676-691
    • Firczuk, M.1    Bochtler, M.2
  • 14
    • 33746648727 scopus 로고    scopus 로고
    • A new D,L-endopeptidase gene product, YojL (renamed CwlS), plays a role in cell separation with LytE and LytF in Bacillus subtilis
    • Fukushima T., Afkham A., Kurosawa S., Tanabe T., Yamamoto H., and Sekiguchi J. A new D,L-endopeptidase gene product, YojL (renamed CwlS), plays a role in cell separation with LytE and LytF in Bacillus subtilis. J. Bacteriol. 188 (2006) 5541-5550
    • (2006) J. Bacteriol. , vol.188 , pp. 5541-5550
    • Fukushima, T.1    Afkham, A.2    Kurosawa, S.3    Tanabe, T.4    Yamamoto, H.5    Sekiguchi, J.6
  • 15
    • 47749111316 scopus 로고    scopus 로고
    • Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities
    • Fyfe P.K., Oza S.L., Fairlamb A.H., and Hunter W.N. Leishmania trypanothione synthetase-amidase structure reveals a basis for regulation of conflicting synthetic and hydrolytic activities. J. Biol. Chem. 283 (2008) 17672-17680
    • (2008) J. Biol. Chem. , vol.283 , pp. 17672-17680
    • Fyfe, P.K.1    Oza, S.L.2    Fairlamb, A.H.3    Hunter, W.N.4
  • 16
    • 33947420470 scopus 로고    scopus 로고
    • New method for fast and accurate binding-site identification and analysis
    • Halgren T. New method for fast and accurate binding-site identification and analysis. Chem. Biol. Drug Des. 69 (2007) 146-148
    • (2007) Chem. Biol. Drug Des. , vol.69 , pp. 146-148
    • Halgren, T.1
  • 17
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L., and Sander C. Dali: a network tool for protein structure comparison. Trends Biochem. Sci. 20 (1995) 478-480
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 20
    • 0035967516 scopus 로고    scopus 로고
    • Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease
    • Khayat R., Batra R., Massariol M.J., Lagace L., and Tong L. Investigating the role of histidine 157 in the catalytic activity of human cytomegalovirus protease. Biochemistry 40 (2001) 6344-6351
    • (2001) Biochemistry , vol.40 , pp. 6344-6351
    • Khayat, R.1    Batra, R.2    Massariol, M.J.3    Lagace, L.4    Tong, L.5
  • 21
    • 0024581874 scopus 로고
    • Identification of an extracellular protein of Listeria monocytogenes possibly involved in intracellular uptake by mammalian cells
    • Kuhn M., and Goebel W. Identification of an extracellular protein of Listeria monocytogenes possibly involved in intracellular uptake by mammalian cells. Infect. Immun. 57 (1989) 55-61
    • (1989) Infect. Immun. , vol.57 , pp. 55-61
    • Kuhn, M.1    Goebel, W.2
  • 23
    • 33645237935 scopus 로고    scopus 로고
    • Skl, a novel choline-binding N-acetylmuramoyl-L-alanine amidase of Streptococcus mitis SK137 containing a CHAP domain
    • Llull D., Lopez R., and Garcia E. Skl, a novel choline-binding N-acetylmuramoyl-L-alanine amidase of Streptococcus mitis SK137 containing a CHAP domain. FEBS Lett. 580 (2006) 1959-1964
    • (2006) FEBS Lett. , vol.580 , pp. 1959-1964
    • Llull, D.1    Lopez, R.2    Garcia, E.3
  • 24
    • 33644852491 scopus 로고    scopus 로고
    • Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges
    • Lu J.Z., Fujiwara T., Komatsuzawa H., Sugai M., and Sakon J. Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges. J. Biol. Chem. 281 (2006) 549-558
    • (2006) J. Biol. Chem. , vol.281 , pp. 549-558
    • Lu, J.Z.1    Fujiwara, T.2    Komatsuzawa, H.3    Sugai, M.4    Sakon, J.5
  • 25
    • 0032954665 scopus 로고    scopus 로고
    • Bacillus subtilis 168 gene lytF encodes a γ-D-glutamate-meso-diaminopimelate muropeptidase expressed by the alternative vegetative sigma factor, σD
    • Margot P., Pagni M., and Karamata D. Bacillus subtilis 168 gene lytF encodes a γ-D-glutamate-meso-diaminopimelate muropeptidase expressed by the alternative vegetative sigma factor, σD. Microbiology 145 (1999) 57-65
    • (1999) Microbiology , vol.145 , pp. 57-65
    • Margot, P.1    Pagni, M.2    Karamata, D.3
  • 26
    • 0036845352 scopus 로고    scopus 로고
    • GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands
    • Marino M., Banerjee M., Jonquieres R., Cossart P., and Ghosh P. GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands. EMBO J. 21 (2002) 5623-5634
    • (2002) EMBO J. , vol.21 , pp. 5623-5634
    • Marino, M.1    Banerjee, M.2    Jonquieres, R.3    Cossart, P.4    Ghosh, P.5
  • 27
    • 0013866537 scopus 로고
    • Biochemistry of bacterial cell walls
    • Martin H.H. Biochemistry of bacterial cell walls. Annu. Rev. Biochem. 35 (1966) 457-484
    • (1966) Annu. Rev. Biochem. , vol.35 , pp. 457-484
    • Martin, H.H.1
  • 28
    • 33646180106 scopus 로고    scopus 로고
    • SH3 domains
    • Cesareni G., Gimona M., Sudol M., and Yaffe M. (Eds), Wiley-VCH Verlag GmbH, Weinheim, Germany
    • Mayer B.J., and Saksella K. SH3 domains. In: Cesareni G., Gimona M., Sudol M., and Yaffe M. (Eds). Modular Protein Domains (2005), Wiley-VCH Verlag GmbH, Weinheim, Germany
    • (2005) Modular Protein Domains
    • Mayer, B.J.1    Saksella, K.2
  • 30
    • 0028961335 scopus 로고
    • SCOP: a structural classification of proteins database for the investigation of sequences and structures
    • Murzin A.G., Brenner S.E., Hubbard T., and Chothia C. SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247 (1995) 536-540
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 31
    • 0035957329 scopus 로고    scopus 로고
    • Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme
    • Nelson D., Loomis L., and Fischetti V.A. Prevention and elimination of upper respiratory colonization of mice by group A streptococci by using a bacteriophage lytic enzyme. Proc. Natl. Acad. Sci. USA 98 (2001) 4107-4112
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4107-4112
    • Nelson, D.1    Loomis, L.2    Fischetti, V.A.3
  • 33
    • 0032964960 scopus 로고    scopus 로고
    • Peptidoglycan hydrolase LytF plays a role in cell separation with CwlF during vegetative growth of Bacillus subtilis
    • Ohnishi R., Ishikawa S., and Sekiguchi J. Peptidoglycan hydrolase LytF plays a role in cell separation with CwlF during vegetative growth of Bacillus subtilis. J. Bacteriol. 181 (1999) 3178-3184
    • (1999) J. Bacteriol. , vol.181 , pp. 3178-3184
    • Ohnishi, R.1    Ishikawa, S.2    Sekiguchi, J.3
  • 34
    • 0343433408 scopus 로고    scopus 로고
    • Cysteine proteases and their inhibitors
    • Otto H.H., and Schirmeister T. Cysteine proteases and their inhibitors. Chem. Rev. 97 (1997) 133-172
    • (1997) Chem. Rev. , vol.97 , pp. 133-172
    • Otto, H.H.1    Schirmeister, T.2
  • 36
    • 0029154488 scopus 로고
    • Why does Escherichia coli recycle its cell wall peptides?
    • Park J.T. Why does Escherichia coli recycle its cell wall peptides?. Mol. Microbiol. 17 (1995) 421-426
    • (1995) Mol. Microbiol. , vol.17 , pp. 421-426
    • Park, J.T.1
  • 37
    • 33745611416 scopus 로고    scopus 로고
    • Gene fusion/fission is a major contributor to evolution of multi-domain bacterial proteins
    • Pasek S., Risler J.L., and Brezellec P. Gene fusion/fission is a major contributor to evolution of multi-domain bacterial proteins. Bioinformatics 22 (2006) 1418-1423
    • (2006) Bioinformatics , vol.22 , pp. 1418-1423
    • Pasek, S.1    Risler, J.L.2    Brezellec, P.3
  • 38
    • 0032555743 scopus 로고    scopus 로고
    • Crystal structure of the Abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions
    • Pisabarro M.T., Serrano L., and Wilmanns M. Crystal structure of the Abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions. J. Mol. Biol. 281 (1998) 513-521
    • (1998) J. Mol. Biol. , vol.281 , pp. 513-521
    • Pisabarro, M.T.1    Serrano, L.2    Wilmanns, M.3
  • 39
    • 0033057517 scopus 로고    scopus 로고
    • Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer
    • Ponting C.P., Aravind L., Schultz J., Bork P., and Koonin E.V. Eukaryotic signalling domain homologues in archaea and bacteria. Ancient ancestry and horizontal gene transfer. J. Mol. Biol. 289 (1999) 729-745
    • (1999) J. Mol. Biol. , vol.289 , pp. 729-745
    • Ponting, C.P.1    Aravind, L.2    Schultz, J.3    Bork, P.4    Koonin, E.V.5
  • 40
    • 4344600526 scopus 로고    scopus 로고
    • The bifunctional peptidoglycan lysin of Streptococcus agalactiae bacteriophage B30
    • Pritchard D.G., Dong S., Baker J.R., and Engler J.A. The bifunctional peptidoglycan lysin of Streptococcus agalactiae bacteriophage B30. Microbiology 150 (2004) 2079-2087
    • (2004) Microbiology , vol.150 , pp. 2079-2087
    • Pritchard, D.G.1    Dong, S.2    Baker, J.R.3    Engler, J.A.4
  • 41
    • 0037727706 scopus 로고    scopus 로고
    • Amidase domains from bacterial and phage autolysins define a family of γ-D,L-glutamate-specific amidohydrolases
    • Rigden D.J., Jedrzejas M.J., and Galperin M.Y. Amidase domains from bacterial and phage autolysins define a family of γ-D,L-glutamate-specific amidohydrolases. Trends Biochem. Sci. 28 (2003) 230-234
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 230-234
    • Rigden, D.J.1    Jedrzejas, M.J.2    Galperin, M.Y.3
  • 42
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer K.H., and Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36 (1972) 407-477
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 43
    • 0020653625 scopus 로고
    • Structure, function, and assembly of cell walls of Gram-positive bacteria
    • Shockman G.D., and Barrett J.F. Structure, function, and assembly of cell walls of Gram-positive bacteria. Annu. Rev. Microbiol. 37 (1983) 501-527
    • (1983) Annu. Rev. Microbiol. , vol.37 , pp. 501-527
    • Shockman, G.D.1    Barrett, J.F.2
  • 44
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: multiple enzymes with multiple functions
    • Smith T.J., Blackman S.A., and Foster S.J. Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology 146 (2000) 249-262
    • (2000) Microbiology , vol.146 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 45
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer A.C., and Menard R. Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol. 244 (1994) 486-500
    • (1994) Methods Enzymol. , vol.244 , pp. 486-500
    • Storer, A.C.1    Menard, R.2
  • 46
    • 0014202386 scopus 로고
    • Mechanisms of enzymatic bacteriolysis. Cell walls of bacteria are solubilized by action of either specific carbohydrases or specific peptidases
    • Strominger J.L., and Ghuysen J.M. Mechanisms of enzymatic bacteriolysis. Cell walls of bacteria are solubilized by action of either specific carbohydrases or specific peptidases. Science 156 (1967) 213-221
    • (1967) Science , vol.156 , pp. 213-221
    • Strominger, J.L.1    Ghuysen, J.M.2
  • 47
    • 0037379280 scopus 로고    scopus 로고
    • Characterization of the Bacillus subtilis ywtD gene, whose product is involved in γ-polyglutamic acid degradation
    • Suzuki T., and Tahara Y. Characterization of the Bacillus subtilis ywtD gene, whose product is involved in γ-polyglutamic acid degradation. J. Bacteriol. 185 (2003) 2379-2382
    • (2003) J. Bacteriol. , vol.185 , pp. 2379-2382
    • Suzuki, T.1    Tahara, Y.2
  • 48
    • 0037224580 scopus 로고    scopus 로고
    • Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the γ-D-glutamyl-meso-diaminopimelate bond in murein peptides
    • Uehara T., and Park J.T. Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the γ-D-glutamyl-meso-diaminopimelate bond in murein peptides. J. Bacteriol. 185 (2003) 679-682
    • (2003) J. Bacteriol. , vol.185 , pp. 679-682
    • Uehara, T.1    Park, J.T.2
  • 49
    • 18944367563 scopus 로고    scopus 로고
    • Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate
    • Uehara T., Suefuji K., Valbuena N., Meehan B., Donegan M., and Park J.T. Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate. J. Bacteriol. 187 (2005) 3643-3649
    • (2005) J. Bacteriol. , vol.187 , pp. 3643-3649
    • Uehara, T.1    Suefuji, K.2    Valbuena, N.3    Meehan, B.4    Donegan, M.5    Park, J.T.6
  • 51
    • 30044442427 scopus 로고    scopus 로고
    • A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis
    • Vivares D., Arnoux P., and Pignol D. A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis. Proc. Natl. Acad. Sci. USA 102 (2005) 18848-18853
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18848-18853
    • Vivares, D.1    Arnoux, P.2    Pignol, D.3
  • 55
    • 6944227521 scopus 로고    scopus 로고
    • Characterization of a new Bacillus subtilis peptidoglycan hydrolase gene, yvcE (named cwlO), and the enzymatic properties of its encoded protein
    • Yamaguchi H., Furuhata K., Fukushima T., Yamamoto H., and Sekiguchi J. Characterization of a new Bacillus subtilis peptidoglycan hydrolase gene, yvcE (named cwlO), and the enzymatic properties of its encoded protein. J. Biosci. Bioeng. 98 (2004) 174-181
    • (2004) J. Biosci. Bioeng. , vol.98 , pp. 174-181
    • Yamaguchi, H.1    Furuhata, K.2    Fukushima, T.3    Yamamoto, H.4    Sekiguchi, J.5
  • 56
    • 0242575014 scopus 로고    scopus 로고
    • Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases
    • Yamamoto H., Kurosawa S., and Sekiguchi J. Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF on the Bacillus subtilis cell surface and stability of these enzymes to cell wall-bound or extracellular proteases. J. Bacteriol. 185 (2003) 6666-6677
    • (2003) J. Bacteriol. , vol.185 , pp. 6666-6677
    • Yamamoto, H.1    Kurosawa, S.2    Sekiguchi, J.3


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