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Volumn 94, Issue 3, 2012, Pages 704-710

S1 pocket fingerprints of human and bacterial methionine aminopeptidases determined using fluorogenic libraries of substrates and phosphorus based inhibitors

Author keywords

Aminopeptidase; Enzyme; Inhibitor; Protease; Substrate library; Substrate specificity

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; METHIONINE; METHIONYL AMINOPEPTIDASE; PEPTIDE HYDROLASE INHIBITOR; PHOSPHINATE DERIVATIVE; PHOSPHINE DERIVATIVE; PHOSPHONIC ACID DERIVATIVE; PHOSPHORUS; UNCLASSIFIED DRUG;

EID: 84857038589     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.10.014     Document Type: Article
Times cited : (17)

References (30)
  • 2
    • 60349090901 scopus 로고    scopus 로고
    • Fine tuning the N-terminal residue excision with methionine analogues
    • B. Wiltschi, L. Merkel, and N. Budisa Fine tuning the N-terminal residue excision with methionine analogues Chembiochem 10 2009 217 220
    • (2009) Chembiochem , vol.10 , pp. 217-220
    • Wiltschi, B.1    Merkel, L.2    Budisa, N.3
  • 3
    • 0023135722 scopus 로고
    • Processing of the initiation methionine from proteins: Properties of the Escherichia coli methionine aminopeptidase and its gene structure
    • A. Ben-Bassat, K. Bauer, S.Y. Chang, K. Myambo, A. Boosman, and S. Chang Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure J. Bacteriol. 169 1987 751 757 (Pubitemid 17010891)
    • (1987) Journal of Bacteriology , vol.169 , Issue.2 , pp. 751-757
    • Ben-Bassat, A.1    Bauer, K.2    Chang, S.-Y.3
  • 4
    • 27744565323 scopus 로고    scopus 로고
    • Structural basis for the functional differences between type I and type II human methionine aminopeptidases
    • DOI 10.1021/bi051691k
    • A. Addlagatta, X. Hu, J.O. Liu, and B.W. Matthews Structural basis for the functional differences between type I and type II human methionine aminopeptidases Biochemistry 44 2005 14741 14749 (Pubitemid 41612254)
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 14741-14749
    • Addlagatta, A.1    Hu, X.2    Liu, J.O.3    Matthews, B.W.4
  • 5
    • 0032127904 scopus 로고    scopus 로고
    • N-terminal processing: The methionine aminopeptidase and N(α)-acetyl transferase families
    • DOI 10.1016/S0968-0004(98)01227-4, PII S0968000498012274
    • R.A. Bradshaw, W.W. Brickey, and K.W. Walker N-terminal processing: the methionine aminopeptidase and N alpha-acetyl transferase families Trends Biochem. Sci. 23 1998 263 267 (Pubitemid 28343371)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.7 , pp. 263-267
    • Bradshaw, R.A.1    Brickey, W.W.2    Walker, K.W.3
  • 6
    • 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
    • W.T. Lowther, A.M. Orville, D.T. Madden, S. Lim, D.H. Rich, and B.W. Matthews Escherichia coli methionine aminopeptidase: implications of crystallographic analyses of the native, mutant, and inhibited enzymes for the mechanism of catalysis Biochemistry 38 1999 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
  • 10
    • 0032515029 scopus 로고    scopus 로고
    • Structure of human methionine aminopeptidase-2 complexed with fumagillin
    • S. Liu, J. Widom, C.W. Kemp, C.M. Crews, and J. Clardy Structure of human methionine aminopeptidase-2 complexed with fumagillin Science 282 1998 1324 1327 (Pubitemid 28524496)
    • (1998) Science , vol.282 , Issue.5392 , pp. 1324-1327
    • Liu, S.1    Widom, J.2    Kemp, C.W.3    Crews, C.M.4    Clardy, J.5
  • 11
    • 0036882401 scopus 로고    scopus 로고
    • Metalloaminopeptidases: Common functional themes in disparate structural surroundings
    • W.T. Lowther, and B.W. Matthews Metalloaminopeptidases: common functional themes in disparate structural surroundings Chem. Rev. 102 2002 4581 4608
    • (2002) Chem. Rev. , vol.102 , pp. 4581-4608
    • Lowther, W.T.1    Matthews, B.W.2
  • 12
    • 33746496094 scopus 로고    scopus 로고
    • Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase
    • DOI 10.1110/ps.062278006
    • A. Addlagatta, and B.W. Matthews Structure of the angiogenesis inhibitor ovalicin bound to its noncognate target, human Type 1 methionine aminopeptidase Protein Sci. 15 2006 1842 1848 (Pubitemid 44141502)
    • (2006) Protein Science , vol.15 , Issue.8 , pp. 1842-1848
    • Addlagatta, A.1    Matthews, B.W.2
  • 14
    • 0025204095 scopus 로고
    • Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth
    • D. Ingber, T. Fujita, S. Kishimoto, K. Sudo, T. Kanamaru, H. Brem, and J. Folkman Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth Nature 348 1990 555 557 (Pubitemid 120015110)
    • (1990) Nature , vol.348 , Issue.6301 , pp. 555-557
    • Ingber, D.1    Fujita, T.2    Kishimoto, S.3    Sudo, K.4    Kanamaru, T.5    Brem, H.6    Folkman, J.7
  • 16
    • 0024347025 scopus 로고
    • Methionine aminopeptidase gene of Escherichia coli is essential for cell growth
    • S.Y. Chang, E.C. McGary, and S. Chang Methionine aminopeptidase gene of Escherichia coli is essential for cell growth J. Bacteriol. 171 1989 4071 4072 (Pubitemid 19174182)
    • (1989) Journal of Bacteriology , vol.171 , Issue.7 , pp. 4071-4072
    • Chang, S.-Y.P.1    McGary, E.C.2    Chang, S.3
  • 17
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • I. Schechter, and A. Berger On the size of the active site in proteases. I. Papain Biochem. Biophys. Res. Commun. 27 1967 157 162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 18
    • 77449129432 scopus 로고    scopus 로고
    • Aminopeptidase fingerprints. An integrated approach for identification of good substrates and optimal inhibitors
    • M. Drag, M. Bogyo, J.A. Ellman, and G.S. Salvesen Aminopeptidase fingerprints. An integrated approach for identification of good substrates and optimal inhibitors J. Biol. Chem. 285 2010 3310 3318
    • (2010) J. Biol. Chem. , vol.285 , pp. 3310-3318
    • Drag, M.1    Bogyo, M.2    Ellman, J.A.3    Salvesen, G.S.4
  • 20
    • 78449282145 scopus 로고    scopus 로고
    • Synthesis of alpha-carboxyphosphinopeptides derived from norleucine
    • J. Picha, M. Budesinsky, P. Fiedler, M. Sanda, and J. Jiracek Synthesis of alpha-carboxyphosphinopeptides derived from norleucine Amino Acids 39 2010 1265 1280
    • (2010) Amino Acids , vol.39 , pp. 1265-1280
    • Picha, J.1    Budesinsky, M.2    Fiedler, P.3    Sanda, M.4    Jiracek, J.5
  • 21
    • 79952757853 scopus 로고    scopus 로고
    • Unusual activity pattern of leucine aminopeptidase inhibitors based on phosphorus containing derivatives of methionine and norleucine
    • J. Picha, R. Liboska, M. Budesinsky, J. Jiracek, M. Pawelczak, and A. Mucha Unusual activity pattern of leucine aminopeptidase inhibitors based on phosphorus containing derivatives of methionine and norleucine J. Enzym. Inhib. Med. Chem. 26 2011 155 161
    • (2011) J. Enzym. Inhib. Med. Chem. , vol.26 , pp. 155-161
    • Picha, J.1    Liboska, R.2    Budesinsky, M.3    Jiracek, J.4    Pawelczak, M.5    Mucha, A.6
  • 26
    • 0035807015 scopus 로고    scopus 로고
    • Steady-state kinetic characterization of substrates and metal-ion specificities of the full-length and N-terminally truncated recombinant human methionine aminopeptidases (Type 2)
    • DOI 10.1021/bi010806r
    • G. Yang, R.B. Kirkpatrick, T. Ho, G.F. Zhang, P.H. Liang, K.O. Johanson, D.J. Casper, M.L. Doyle, J.P. Marino Jr., S.K. Thompson, W. Chen, D.G. Tew, and T.D. Meek Steady-state kinetic characterization of substrates and metal-ion specificities of the full-length and N-terminally truncated recombinant human methionine aminopeptidases (type 2) Biochemistry 40 2001 10645 10654 (Pubitemid 32816677)
    • (2001) Biochemistry , vol.40 , Issue.35 , pp. 10645-10654
    • Yang, G.1    Kirkpatrick, R.B.2    Ho, T.3    Zhang, G.-F.4    Liang, P.-H.5    Johanson, K.O.6    Casper, D.J.7    Doyle, M.L.8    Marino Jr., J.P.9    Thompson, S.K.10    Chen, W.11    Tew, D.G.12    Meek, T.D.13
  • 27
    • 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
    • W.T. Lowther, Y. Zhang, P.B. Sampson, J.F. Honek, and B.W. Matthews Insights into the mechanism of Escherichia coli methionine aminopeptidase from the structural analysis of reaction products and phosphorus-based transition-state analogues Biochemistry 38 1999 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
  • 29
    • 77956310878 scopus 로고    scopus 로고
    • Emerging principles in protease-based drug discovery
    • M. Drag, and G.S. Salvesen Emerging principles in protease-based drug discovery Nat. Rev. Drug Discov. 9 2010 690 701
    • (2010) Nat. Rev. Drug Discov. , vol.9 , pp. 690-701
    • Drag, M.1    Salvesen, G.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.