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Volumn 47, Issue 6, 2004, Pages 1325-1328

Crystal Structures of Staphylococcus aureus Methionine Aminopeptidase Complexed with Keto Heterocycle and Aminoketone Inhibitors Reveal the Formation of a Tetrahedral Intermediate

Author keywords

[No Author keywords available]

Indexed keywords

AMINOKETONE; ANTIINFECTIVE AGENT; BACTERIAL ENZYME; ENZYME INHIBITOR; HETEROCYCLIC COMPOUND; METHIONYL AMINOPEPTIDASE; METHIONYL AMINOPEPTIDASE INHIBITOR; UNCLASSIFIED DRUG; AMINE; AMINOPEPTIDASE; CYCLOPROPANE DERIVATIVE; KETONE; PYRIDINE DERIVATIVE; THIAZOLE DERIVATIVE;

EID: 1542298116     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm034188j     Document Type: Article
Times cited : (44)

References (34)
  • 1
    • 0037413729 scopus 로고    scopus 로고
    • Control of protein life-span by N-terminal methionine excision
    • Giglione, C.; Vallon, O.; Meinnel, T. Control of protein life-span by N-terminal methionine excision. EMBO J. 2003, 22, 13-23.
    • (2003) EMBO J. , vol.22 , pp. 13-23
    • Giglione, C.1    Vallon, O.2    Meinnel, T.3
  • 2
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • Hirel, P. H.; Schmitter, M. J.; Dessen, P.; Fayat, G.; Blanquet, S. Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid. Proc. Natl. Acad. Sci. U.S.A. 1989, 86, 8247-8251.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, M.J.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 3
    • 0025200973 scopus 로고
    • The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation
    • Moerschell, R. P.; Hosokawa, Y.; Tsunasawa, S.; Sherman, F. The specificities of yeast methionine aminopeptidase and acetylation of amino-terminal methionine in vivo. Processing of altered iso-1-cytochromes c created by oligonucleotide transformation. J. Biol. Chem. 1990, 265, 19638-19643.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19638-19643
    • Moerschell, R.P.1    Hosokawa, Y.2    Tsunasawa, S.3    Sherman, F.4
  • 4
    • 0001530324 scopus 로고
    • The NH2 terminal residue of the proteins from cell-free extract of E. coli
    • Waller, J. P. The NH2 terminal residue of the proteins from cell-free extract of E. coli. J. Mol. Biol. 1963, 7, 483-496.
    • (1963) J. Mol. Biol. , vol.7 , pp. 483-496
    • Waller, J.P.1
  • 5
    • 0024347025 scopus 로고
    • Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
    • Chang, S. Y.; McGary, E. C.; Chang, S. Methionine aminopeptidase gene of Escherichia coli is essential for cell growth. J. Bacteriol. 1989, 171, 4071-4072.
    • (1989) J. Bacteriol. , vol.171 , pp. 4071-4072
    • Chang, S.Y.1    McGary, E.C.2    Chang, S.3
  • 6
    • 0029585125 scopus 로고
    • Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases
    • Li, X.; Chang, Y. H. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 12357-12361.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 12357-12361
    • Li, X.1    Chang, Y.H.2
  • 7
    • 0024729628 scopus 로고
    • pepM is an essential gene in Salmonella typhimurium
    • Miller, C. G.; Kukral, A. M.; Miller, J. L.; Movva, N. R. pepM is an essential gene in Salmonella typhimurium. J. Bacteriol. 1989, 171, 5215-5217.
    • (1989) J. Bacteriol. , vol.171 , pp. 5215-5217
    • Miller, C.G.1    Kukral, A.M.2    Miller, J.L.3    Movva, N.R.4
  • 8
    • 0013292073 scopus 로고    scopus 로고
    • Methionine aminopeptidases and angiogenesis
    • Bradshaw, R. A.; Yi, E. Methionine aminopeptidases and angiogenesis. Essays Biochem. 2002, 38, 65-78.
    • (2002) Essays Biochem. , vol.38 , pp. 65-78
    • Bradshaw, R.A.1    Yi, E.2
  • 9
    • 0025204095 scopus 로고
    • Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth
    • Ingber, D.; Fujita, T.; Kishimoto, S.; Sudo, K.; Kanamaru, T.; Brem, H.; Folkman, J. Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth. Nature 1990, 348, 555-557.
    • (1990) Nature , vol.348 , pp. 555-557
    • Ingber, D.1    Fujita, T.2    Kishimoto, S.3    Sudo, K.4    Kanamaru, T.5    Brem, H.6    Folkman, J.7
  • 10
    • 0030924753 scopus 로고    scopus 로고
    • The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2
    • Sin, N.; Meng, L.; Wang, M. Q.; Wen, J. J.; Bornmann, W. G.; Crews, C. M. The anti-angiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 6099-6103.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6099-6103
    • Sin, N.1    Meng, L.2    Wang, M.Q.3    Wen, J.J.4    Bornmann, W.G.5    Crews, C.M.6
  • 11
    • 0033564306 scopus 로고    scopus 로고
    • Escherichia coli methionine aminopeptidase: Implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis
    • Lowther, W. T.; Orville, A. M.; Madden, D. T.; Lim, S.; Rich, D. H.; Matthews, B. W. Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis. Biochemistry 1999, 38, 7678-7688.
    • (1999) Biochemistry , vol.38 , pp. 7678-7688
    • Lowther, W.T.1    Orville, A.M.2    Madden, D.T.3    Lim, S.4    Rich, D.H.5    Matthews, B.W.6
  • 13
    • 0033539594 scopus 로고    scopus 로고
    • Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues
    • Lowther, W. T.; Zhang, Y.; Sampson, P. B.; Honek, J. F.; Matthews, B. W. Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues. Biochemistry 1999, 38, 14810-14819.
    • (1999) Biochemistry , vol.38 , pp. 14810-14819
    • Lowther, W.T.1    Zhang, Y.2    Sampson, P.B.3    Honek, J.F.4    Matthews, B.W.5
  • 15
    • 0033600583 scopus 로고    scopus 로고
    • The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme
    • D'souza, V. M.; Holz, R. C. The methionyl aminopeptidase from Escherichia coli can function as an iron(II) enzyme. Biochemistry 1999, 38, 11079-11085.
    • (1999) Biochemistry , vol.38 , pp. 11079-11085
    • D'souza, V.M.1    Holz, R.C.2
  • 17
    • 0031703555 scopus 로고    scopus 로고
    • 2+ as a cofactor: A case of mistaken identity?
    • 2+ as a cofactor: a case of mistaken identity? Protein Sci. 1998, 7, 2684-2687.
    • (1998) Protein Sci. , vol.7 , pp. 2684-2687
    • Walker, K.W.1    Bradshaw, R.A.2
  • 19
    • 0020399342 scopus 로고
    • α-Aminoaldehydes: Transition state analogue inhibitors of leucine aminopeptidase
    • Andersson, L.; Isley, T. C.; Wolfenden, R. α-Aminoaldehydes: Transition state analogue inhibitors of leucine aminopeptidase. Biochemistry 1982, 21, 4177-4180.
    • (1982) Biochemistry , vol.21 , pp. 4177-4180
    • Andersson, L.1    Isley, T.C.2    Wolfenden, R.3
  • 20
    • 0025102977 scopus 로고
    • Inhibition of cathepsin B and papain by peptidyl alpha-keto esters, alpha-keto amides, alpha-diketones, and alpha-keto acids
    • Hu, L. Y.; Abeles, R. H. Inhibition of cathepsin B and papain by peptidyl alpha-keto esters, alpha-keto amides, alpha-diketones, and alpha-keto acids. Arch. Biochem. Biophys. 1990, 281, 271-274.
    • (1990) Arch. Biochem. Biophys. , vol.281 , pp. 271-274
    • Hu, L.Y.1    Abeles, R.H.2
  • 21
    • 0017747506 scopus 로고
    • Interaction of papain with derivatives of phenylalanylglycinal
    • Mattis, J. A.; Henes, J. B.; Fruton, J. S. Interaction of papain with derivatives of phenylalanylglycinal. J. Biol. Chem. 1977, 252, 6776-6782.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6776-6782
    • Mattis, J.A.1    Henes, J.B.2    Fruton, J.S.3
  • 22
    • 0022504190 scopus 로고
    • Design and synthesis of potent and specific renin inhibitors containing difluorostatine, difluorostatone, and related analogues
    • Thaisrivongs, S.; Pals, D. T.; Kati, W. M.; Turner, S. R.; Thomasco, L. M.; Watt, W. Design and synthesis of potent and specific renin inhibitors containing difluorostatine, difluorostatone, and related analogues. J. Med. Chem. 1986, 29, 2080-2087.
    • (1986) J. Med. Chem. , vol.29 , pp. 2080-2087
    • Thaisrivongs, S.1    Pals, D.T.2    Kati, W.M.3    Turner, S.R.4    Thomasco, L.M.5    Watt, W.6
  • 23
    • 0020393784 scopus 로고
    • Low-molecular-weight enzyme inhibitors of microbial origin
    • Umezawa, H. Low-molecular-weight enzyme inhibitors of microbial origin. Annu. Rev. Microbiol. 1982, 36, 75-99.
    • (1982) Annu. Rev. Microbiol. , vol.36 , pp. 75-99
    • Umezawa, H.1
  • 26
    • 0035397393 scopus 로고    scopus 로고
    • Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: New ways of analysing data
    • Cortes, A.; Cascante, M.; Cardenas, M. L.; Cornish-Bowden, A. Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: new ways of analysing data. Biochem. J. 2001, 357, 263-268.
    • (2001) Biochem. J. , vol.357 , pp. 263-268
    • Cortes, A.1    Cascante, M.2    Cardenas, M.L.3    Cornish-Bowden, A.4
  • 27
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • Liu, S.; Widom, J.; Kemp, C. W.; Crews, C. M.; Clardy, J. Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science 1998, 282, 1324-1327.
    • (1998) Science , vol.282 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Crews, C.M.4    Clardy, J.5
  • 29
  • 31
    • 0028134635 scopus 로고
    • Synthesis and structure-activity relationships of peptidyl α-keto heterocycles as novel inhibitors of prolyl endopeptidase
    • Tsutsumi, S.; Okonogi, T.; Shibahara, S.; Ohuchi, S.; Hatsushiba, E.; Patchett, A. A.; Christensen, B. G. Synthesis and structure-activity relationships of peptidyl α-keto heterocycles as novel inhibitors of prolyl endopeptidase. J. Med. Chem. 1994, 37, 3492-3502.
    • (1994) J. Med. Chem. , vol.37 , pp. 3492-3502
    • Tsutsumi, S.1    Okonogi, T.2    Shibahara, S.3    Ohuchi, S.4    Hatsushiba, E.5    Patchett, A.A.6    Christensen, B.G.7
  • 32
    • 0035818432 scopus 로고    scopus 로고
    • Structural evidence that the methionyl Aminopeptidase from Escherichia coli is a mononuclear metalloprotease
    • Cosper, N. J.; D'souza, V. M.; Scott, R. A.; Holz, R. C. Structural evidence that the methionyl Aminopeptidase from Escherichia coli is a mononuclear metalloprotease. Biochemistry 2001, 40, 13302-13309.
    • (2001) Biochemistry , vol.40 , pp. 13302-13309
    • Cosper, N.J.1    D'souza, V.M.2    Scott, R.A.3    Holz, R.C.4
  • 33
    • 0029879577 scopus 로고    scopus 로고
    • Synthesis, structure, and structure-activity relationships of divalent thrombin inhibitors containing an alpha-keto-amide transition-state mimetic
    • Krishnan, R.; Tulinsky, A.; Vlasuk, G. P.; Pearson, D.; Vallar, P.; Bergum, P.; Brunck, T. K.; Ripka, W. C. Synthesis, structure, and structure-activity relationships of divalent thrombin inhibitors containing an alpha-keto-amide transition-state mimetic. Protein Sci. 1996, 5, 422-433.
    • (1996) Protein Sci. , vol.5 , pp. 422-433
    • Krishnan, R.1    Tulinsky, A.2    Vlasuk, G.P.3    Pearson, D.4    Vallar, P.5    Bergum, P.6    Brunck, T.K.7    Ripka, W.C.8
  • 34
    • 0038521576 scopus 로고    scopus 로고
    • Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli
    • Copik, A. J.; Swierczek, S. I.; Lowther, W. T.; D'souza, V. M.; Matthews, B. W.; Holz, R. C. Kinetic and spectroscopic characterization of the H178A methionyl aminopeptidase from Escherichia coli. Biochemistry 2003, 42, 6283-6292.
    • (2003) Biochemistry , vol.42 , pp. 6283-6292
    • Copik, A.J.1    Swierczek, S.I.2    Lowther, W.T.3    D'souza, V.M.4    Matthews, B.W.5    Holz, R.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.