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Volumn 353, Issue 3, 2007, Pages 706-712

Characterization and role of Peptidase N from Salmonella enterica serovar Typhimurium

Author keywords

Aminopeptidase; Cellular proteolysis; M1 peptidase; Stress; Substrate specificity

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMINOPEPTIDASE; N ETHYLMALEIMIDE; PEPTIDASE; PEPTIDASE N; UNCLASSIFIED DRUG;

EID: 33846013178     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.12.073     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 6344252715 scopus 로고    scopus 로고
    • Comparative genomics and functional roles of the ATP dependent proteases Lon and Clp during cytosolic protein degradation
    • Chandu D., and Nandi D. Comparative genomics and functional roles of the ATP dependent proteases Lon and Clp during cytosolic protein degradation. Res. Microbiol. 155 (2004) 710-719
    • (2004) Res. Microbiol. , vol.155 , pp. 710-719
    • Chandu, D.1    Nandi, D.2
  • 2
    • 0030200482 scopus 로고    scopus 로고
    • Bacterial aminopeptidases: properties and functions
    • Gonzales T., and Robert-Baudouy J. Bacterial aminopeptidases: properties and functions. FEMS Microbiol. Rev. 18 (1996) 319-344
    • (1996) FEMS Microbiol. Rev. , vol.18 , pp. 319-344
    • Gonzales, T.1    Robert-Baudouy, J.2
  • 3
    • 0037458547 scopus 로고    scopus 로고
    • PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya. Implications in cytosolic protein degradation
    • Chandu D., Kumar A., and Nandi D. PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya. Implications in cytosolic protein degradation. J .Biol.Chem. 278 (2003) 5548-5556
    • (2003) J .Biol.Chem. , vol.278 , pp. 5548-5556
    • Chandu, D.1    Kumar, A.2    Nandi, D.3
  • 4
    • 0034987779 scopus 로고    scopus 로고
    • Male reproductive defects caused by puromycin-sensitive aminopeptidase deficiency in mice
    • Osada T., Watanabe G., Kondo S., Toyoda M., Sakaki Y., and Takeuchi T. Male reproductive defects caused by puromycin-sensitive aminopeptidase deficiency in mice. Mol. Endocrinol. 15 (2001) 960-971
    • (2001) Mol. Endocrinol. , vol.15 , pp. 960-971
    • Osada, T.1    Watanabe, G.2    Kondo, S.3    Toyoda, M.4    Sakaki, Y.5    Takeuchi, T.6
  • 5
    • 0034982609 scopus 로고    scopus 로고
    • Puromycin-sensitive aminopeptidase is essential for the maternal recognition of pregnancy in mice
    • Osada T., Watanabe G., Sakaki Y., and Takeuchi T. Puromycin-sensitive aminopeptidase is essential for the maternal recognition of pregnancy in mice. Mol. Endocrinol. 15 (2001) 882-893
    • (2001) Mol. Endocrinol. , vol.15 , pp. 882-893
    • Osada, T.1    Watanabe, G.2    Sakaki, Y.3    Takeuchi, T.4
  • 7
    • 33746215297 scopus 로고    scopus 로고
    • Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation
    • York I.A., Bhutani N., Zendzian S., Goldberg A.L., and Rock K.L. Tripeptidyl peptidase II is the major peptidase needed to trim long antigenic precursors, but is not required for most MHC class I antigen presentation. J. Immunol. 177 (2006) 1434-1443
    • (2006) J. Immunol. , vol.177 , pp. 1434-1443
    • York, I.A.1    Bhutani, N.2    Zendzian, S.3    Goldberg, A.L.4    Rock, K.L.5
  • 8
    • 0034615568 scopus 로고    scopus 로고
    • Structure and function of the methionine aminopeptidases
    • Lowther W.T., and Matthews B.W. Structure and function of the methionine aminopeptidases. Biochim. Biophys. Acta 1477 (2000) 157-167
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 157-167
    • Lowther, W.T.1    Matthews, B.W.2
  • 9
    • 0024347025 scopus 로고
    • Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
    • Chang S.Y., McGary E.C., and Chang S. Methionine aminopeptidase gene of Escherichia coli is essential for cell growth. J. Bacteriol. 171 (1989) 4071-4072
    • (1989) J. Bacteriol. , vol.171 , pp. 4071-4072
    • Chang, S.Y.1    McGary, E.C.2    Chang, S.3
  • 10
    • 0029585125 scopus 로고
    • Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases
    • Li X., and Chang Y.H. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl. Acad. Sci. USA 92 (1995) 12357-12361
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12357-12361
    • Li, X.1    Chang, Y.H.2
  • 11
    • 0018148676 scopus 로고
    • Peptidase-deficient mutants of Escherichia coli
    • Miller C.G., and Schwartz G. Peptidase-deficient mutants of Escherichia coli. J. Bacteriol. 135 (1978) 603-611
    • (1978) J. Bacteriol. , vol.135 , pp. 603-611
    • Miller, C.G.1    Schwartz, G.2
  • 12
    • 0016208993 scopus 로고
    • Peptidase mutants of Salmonella typhimurium
    • Miller C.G., and Mackinnon K. Peptidase mutants of Salmonella typhimurium. J. Bacteriol. 120 (1974) 355-363
    • (1974) J. Bacteriol. , vol.120 , pp. 355-363
    • Miller, C.G.1    Mackinnon, K.2
  • 14
    • 0033994940 scopus 로고    scopus 로고
    • Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase
    • Lassy R.A., and Miller C.G. Peptidase E, a peptidase specific for N-terminal aspartic dipeptides, is a serine hydrolase. J. Bacteriol. 182 (2000) 2536-2543
    • (2000) J. Bacteriol. , vol.182 , pp. 2536-2543
    • Lassy, R.A.1    Miller, C.G.2
  • 15
    • 0034129876 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids
    • Mathew Z., Knox T.M., and Miller C.G. Salmonella enterica serovar Typhimurium peptidase B is a leucyl aminopeptidase with specificity for acidic amino acids. J. Bacteriol. 182 (2000) 3383-3393
    • (2000) J. Bacteriol. , vol.182 , pp. 3383-3393
    • Mathew, Z.1    Knox, T.M.2    Miller, C.G.3
  • 16
    • 0035040994 scopus 로고    scopus 로고
    • Aspartic peptide hydrolases in Salmonella enterica serovar Typhimurium
    • Larsen R.A., Knox T.M., and Miller C.G. Aspartic peptide hydrolases in Salmonella enterica serovar Typhimurium. J. Bacteriol. 183 (2001) 3089-3097
    • (2001) J. Bacteriol. , vol.183 , pp. 3089-3097
    • Larsen, R.A.1    Knox, T.M.2    Miller, C.G.3
  • 18
    • 0034687682 scopus 로고    scopus 로고
    • The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad
    • Hakansson K., Wang A.H., and Miller C.G. The structure of aspartyl dipeptidase reveals a unique fold with a Ser-His-Glu catalytic triad. Proc. Natl. Acad. Sci. USA 97 (2000) 14097-14102
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 14097-14102
    • Hakansson, K.1    Wang, A.H.2    Miller, C.G.3
  • 19
    • 0346882657 scopus 로고    scopus 로고
    • PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress
    • Chandu D., and Nandi D. PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress. Microbiology 149 (2003) 3437-3447
    • (2003) Microbiology , vol.149 , pp. 3437-3447
    • Chandu, D.1    Nandi, D.2
  • 20
    • 33748629692 scopus 로고    scopus 로고
    • Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site
    • Addlagatta A., Gay L., and Matthews B.W. Structure of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site. Proc. Natl. Acad. Sci. USA 103 (2006) 13339-13344
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13339-13344
    • Addlagatta, A.1    Gay, L.2    Matthews, B.W.3
  • 21
    • 33845954688 scopus 로고    scopus 로고
    • Aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli: Crystal structure and conformational change of the methionine 260 residue involved in substrate recognition
    • Ito K., Nakajima Y., Onohara Y., Takeo M., Nakashima K., Matsubara F., Ito T., and Yoshimoto T. Aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli: Crystal structure and conformational change of the methionine 260 residue involved in substrate recognition. J. Biol. Chem. 281 (2006) 33664-33676
    • (2006) J. Biol. Chem. , vol.281 , pp. 33664-33676
    • Ito, K.1    Nakajima, Y.2    Onohara, Y.3    Takeo, M.4    Nakashima, K.5    Matsubara, F.6    Ito, T.7    Yoshimoto, T.8
  • 22
    • 0023145056 scopus 로고
    • The energy utilized in protein breakdown by the ATP-dependent Protease (La) from Escherichia coli
    • Menon A.S., Waxman L., and Goldberg A.L. The energy utilized in protein breakdown by the ATP-dependent Protease (La) from Escherichia coli. J. Biol. Chem. 262 (1987) 722-726
    • (1987) J. Biol. Chem. , vol.262 , pp. 722-726
    • Menon, A.S.1    Waxman, L.2    Goldberg, A.L.3
  • 24
    • 0032567040 scopus 로고    scopus 로고
    • The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation
    • Tamura N., Lottspeich F., Baumeister W., and Tamura T. The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation. Cell 95 (1998) 637-648
    • (1998) Cell , vol.95 , pp. 637-648
    • Tamura, N.1    Lottspeich, F.2    Baumeister, W.3    Tamura, T.4
  • 25
    • 0027322430 scopus 로고
    • Isolation and characterization of AAP1. A gene encoding an alanine/arginine aminopeptidase in yeast
    • Caprioglio D.R., Padilla C., and Werner-Washburne M. Isolation and characterization of AAP1. A gene encoding an alanine/arginine aminopeptidase in yeast. J. Biol. Chem. 268 (1993) 14310-14315
    • (1993) J. Biol. Chem. , vol.268 , pp. 14310-14315
    • Caprioglio, D.R.1    Padilla, C.2    Werner-Washburne, M.3
  • 27
    • 0020627683 scopus 로고
    • Intracellular activation of albomycin in Escherichia coli and Salmonella typhimurium
    • Braun V., Gunthner K., Hantke K., and Zimmermann L. Intracellular activation of albomycin in Escherichia coli and Salmonella typhimurium. J. Bacteriol. 156 (1983) 308-315
    • (1983) J. Bacteriol. , vol.156 , pp. 308-315
    • Braun, V.1    Gunthner, K.2    Hantke, K.3    Zimmermann, L.4
  • 28
    • 0019139986 scopus 로고
    • Peptide accumulation during growth of peptidase deficient mutants
    • Yen C., Green L., and Miller C.G. Peptide accumulation during growth of peptidase deficient mutants. J. Mol. Biol. 143 (1980) 21-33
    • (1980) J. Mol. Biol. , vol.143 , pp. 21-33
    • Yen, C.1    Green, L.2    Miller, C.G.3
  • 29
    • 0035958678 scopus 로고    scopus 로고
    • Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli
    • Kuroda A., Nomura K., Ohtomo R., Kato J., Ikeda T., Takiguchi N., Ohtake H., and Kornberg A. Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli. Science 293 (2001) 705-708
    • (2001) Science , vol.293 , pp. 705-708
    • Kuroda, A.1    Nomura, K.2    Ohtomo, R.3    Kato, J.4    Ikeda, T.5    Takiguchi, N.6    Ohtake, H.7    Kornberg, A.8
  • 30
    • 26244450607 scopus 로고    scopus 로고
    • Salmonella stress management and its relevance to behaviour during intestinal colonisation and infection
    • Rychlik I., and Barrow P.A. Salmonella stress management and its relevance to behaviour during intestinal colonisation and infection. FEMS. Microbiol. Rev. 29 (2005) 1021-1040
    • (2005) FEMS. Microbiol. Rev. , vol.29 , pp. 1021-1040
    • Rychlik, I.1    Barrow, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.