메뉴 건너뛰기




Volumn 1479, Issue 1-2, 2000, Pages 114-122

Engineering of substrate mimetics as novel-type substrates for glutamic acid-specific endopeptidases: Design, synthesis, and application

Author keywords

Acyl transfer; BL GSE; Enzyme specificity; Substrate mimetics; V8 protease

Indexed keywords

ISOENZYME; PROTEINASE;

EID: 0034659671     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00016-9     Document Type: Article
Times cited : (21)

References (21)
  • 1
    • 33748226769 scopus 로고
    • Protease-catalyzed kinetically controlled peptide synthesis
    • Schellenberger V., Jakubke H.-D. Protease-catalyzed kinetically controlled peptide synthesis. Angew. Chem. Int. Ed. Engl. 30:1991;1437-1449.
    • (1991) Angew. Chem. Int. Ed. Engl. , vol.30 , pp. 1437-1449
    • Schellenberger, V.1    Jakubke, H.-D.2
  • 2
    • 0024382916 scopus 로고
    • Enzymatic catalysts in organic synthesis
    • Wong C.-H. Enzymatic catalysts in organic synthesis. Science. 244:1989;1145-1152.
    • (1989) Science , vol.244 , pp. 1145-1152
    • Wong, C.-H.1
  • 3
    • 0028518514 scopus 로고
    • A designed peptide ligase for total synthesis of Ribonuclease A with unnatural catalytic residues
    • Jackson D.Y., Burnier J., Quan C., Stanley M., Tom J., Wells J.A. A designed peptide ligase for total synthesis of Ribonuclease A with unnatural catalytic residues. Science. 266:1994;243-247.
    • (1994) Science , vol.266 , pp. 243-247
    • Jackson, D.Y.1    Burnier, J.2    Quan, C.3    Stanley, M.4    Tom, J.5    Wells, J.A.6
  • 4
    • 0026416821 scopus 로고
    • Protease-catalyzed peptide synthesis using inverse substrates: The influence of reaction conditions on the trypsin acyl transfer efficiency
    • Schellenberger V., Jakubke H.-D., Zapevalova N.P., Mitin Y.V. Protease-catalyzed peptide synthesis using inverse substrates: the influence of reaction conditions on the trypsin acyl transfer efficiency. Biotechnol. Bioeng. 38:1991;104-108.
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 104-108
    • Schellenberger, V.1    Jakubke, H.-D.2    Zapevalova, N.P.3    Mitin, Y.V.4
  • 5
    • 0002859477 scopus 로고
    • Protease catalyzed peptide synthesis using inverse substrates
    • in: E. Giralt, D. Andreu (Eds.), ESCOM, Leiden
    • Y.V. Mitin, V. Schellenberger, U. Schellenberger, H.-D. Jakubke, N.P. Zapevalova, Protease catalyzed peptide synthesis using inverse substrates, in: E. Giralt, D. Andreu (Eds.), Peptides, ESCOM, Leiden, 1990, pp. 287-288.
    • (1990) Peptides , pp. 287-288
    • Mitin, Y.V.1    Schellenberger, V.2    Schellenberger, U.3    Jakubke, H.-D.4    Zapevalova, N.P.5
  • 6
    • 0029745765 scopus 로고    scopus 로고
    • Trypsin-catalyzed peptide synthesis with various p-guanidinophenyl ester as acyl donors
    • Sekizaki H., Itoh K., Toyota E., Tanizawa K. Trypsin-catalyzed peptide synthesis with various p-guanidinophenyl ester as acyl donors. Chem. Pharm. Bull. 44:1996;1585-1587.
    • (1996) Chem. Pharm. Bull. , vol.44 , pp. 1585-1587
    • Sekizaki, H.1    Itoh, K.2    Toyota, E.3    Tanizawa, K.4
  • 7
    • 0031457134 scopus 로고    scopus 로고
    • Substrate mimetic-mediated peptide synthesis: An irreversible ligation strategy that is independent of substrate specificity
    • Bordusa F., Ullmann D., Elsner C., Jakubke H.-D. Substrate mimetic-mediated peptide synthesis: an irreversible ligation strategy that is independent of substrate specificity. Angew. Chem. Int. Ed. Engl. 36:1997;2473-2475.
    • (1997) Angew. Chem. Int. Ed. Engl. , vol.36 , pp. 2473-2475
    • Bordusa, F.1    Ullmann, D.2    Elsner, C.3    Jakubke, H.-D.4
  • 8
    • 0033545841 scopus 로고    scopus 로고
    • Protease-catalyzed hydrolysis of substrate mimetics (inverse substrates): A new approach reveals a new mechanism
    • Thormann M., Thust S., Hofmann H.-J., Bordusa F. Protease-catalyzed hydrolysis of substrate mimetics (inverse substrates): a new approach reveals a new mechanism. Biochemistry. 38:1999;6056-6062.
    • (1999) Biochemistry , vol.38 , pp. 6056-6062
    • Thormann, M.1    Thust, S.2    Hofmann, H.-J.3    Bordusa, F.4
  • 9
    • 0032989485 scopus 로고    scopus 로고
    • Programming of enzyme specificity by substrate mimetics investigations on the Glu-specific V8 protease reveals a novel general principle of biocatalysis
    • Wehofsky N., Bordusa F. Programming of enzyme specificity by substrate mimetics investigations on the Glu-specific V8 protease reveals a novel general principle of biocatalysis. FEBS Lett. 443:1999;220-224.
    • (1999) FEBS Lett. , vol.443 , pp. 220-224
    • Wehofsky, N.1    Bordusa, F.2
  • 10
    • 0026601661 scopus 로고
    • Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis
    • Svendsen I., Breddam K. Isolation and amino acid sequence of a glutamic acid specific endopeptidase from Bacillus licheniformis. Eur. J. Biochem. 204:1992;165-171.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 165-171
    • Svendsen, I.1    Breddam, K.2
  • 11
    • 0020941316 scopus 로고
    • Proteinase affinity chromatography on bacitracin-sepharose
    • Stepanov V.M., Rudenskaya G.N. Proteinase affinity chromatography on bacitracin-sepharose. J. Appl. Biochem. 5:1983;420-428.
    • (1983) J. Appl. Biochem. , vol.5 , pp. 420-428
    • Stepanov, V.M.1    Rudenskaya, G.N.2
  • 12
    • 0342687552 scopus 로고
    • Optimization of protease-catalyzed acyl transfer reactions. Determination of the partition constant characterizing nucleophile efficiency
    • Schellenberger V., Schuster M., Jakubke H.-D. Optimization of protease-catalyzed acyl transfer reactions. Determination of the partition constant characterizing nucleophile efficiency. Biocatalysis. 4:1990;105-111.
    • (1990) Biocatalysis , vol.4 , pp. 105-111
    • Schellenberger, V.1    Schuster, M.2    Jakubke, H.-D.3
  • 13
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27:1967;157-167.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-167
    • Schechter, I.1    Berger, A.2
  • 14
    • 0342559401 scopus 로고    scopus 로고
    • PhD Thesis, University of Leipzig
    • C. Elsner, PhD Thesis, University of Leipzig, 1999.
    • (1999)
    • Elsner, C.1
  • 15
    • 0015523789 scopus 로고
    • Purification and properties of an extracellular protease of Staphylococcus aureus
    • Drapeau G.R., Boily Y., Houmard J. Purification and properties of an extracellular protease of Staphylococcus aureus. J. Biol. Chem. 247:1972;6720-6726.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6720-6726
    • Drapeau, G.R.1    Boily, Y.2    Houmard, J.3
  • 16
    • 0029041259 scopus 로고
    • Peptide thioester substrates for serine peptidases and metalloendopeptidases
    • in: A.J. Barrett (Ed.), Academic Press
    • J.R. Powers, C.M. Kam, Peptide thioester substrates for serine peptidases and metalloendopeptidases, in: A.J. Barrett (Ed.), Proteolytic Enzymes: Aspartic and Metallo Peptidases, Vol. 248, Academic Press, 1995, pp. 3-18.
    • (1995) Proteolytic Enzymes: Aspartic and Metallo Peptidases , vol.248 , pp. 3-18
    • Powers, J.R.1    Kam, C.M.2
  • 17
    • 0030816077 scopus 로고    scopus 로고
    • Peptide synthesis from N- To C-terminus: An advantageous strategy using protease catalysis
    • Bordusa F., Ullmann D., Jakubke H.-D. Peptide synthesis from N- to C-terminus: an advantageous strategy using protease catalysis. Angew. Chem. Int. Ed. Engl. 36:1997;1099-1101.
    • (1997) Angew. Chem. Int. Ed. Engl. , vol.36 , pp. 1099-1101
    • Bordusa, F.1    Ullmann, D.2    Jakubke, H.-D.3
  • 18
    • 0026503259 scopus 로고
    • Substrate preferences of glutamic acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching
    • Breddam K., Meldal M. Substrate preferences of glutamic acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. Eur. J. Biochem. 206:1992;103-107.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 103-107
    • Breddam, K.1    Meldal, M.2
  • 20
    • 0001073025 scopus 로고
    • Die Partitionskonstante als Effizienzparameter von Nukleophilen bei enzymkatalysierten kinetisch kontrollierten Peptidsynthesen
    • Könnecke A., Schellenberger V., Hofmann H.-J., Jakubke H.-D. Die Partitionskonstante als Effizienzparameter von Nukleophilen bei enzymkatalysierten kinetisch kontrollierten Peptidsynthesen. Pharmazie. 39:1984;785-786.
    • (1984) Pharmazie , vol.39 , pp. 785-786
    • Könnecke, A.1    Schellenberger, V.2    Hofmann, H.-J.3    Jakubke, H.-D.4
  • 21
    • 0030688025 scopus 로고    scopus 로고
    • Subsite specificity studies on the unusual cysteine protease clostripain: Charged residues in the P3 position indicate a narrow subsite region
    • Bordusa F., Ullmann D., Jakubke H.-D. Subsite specificity studies on the unusual cysteine protease clostripain: charged residues in the P3 position indicate a narrow subsite region. Biol. Chem. 378:1997;1193-1198.
    • (1997) Biol. Chem. , vol.378 , pp. 1193-1198
    • Bordusa, F.1    Ullmann, D.2    Jakubke, H.-D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.