메뉴 건너뛰기




Volumn 33, Issue 5, 1996, Pages 281-286

Clostripain linker deletion variants yield active enzyme in Escherichia coli: A possible function of the linker peptide as intramolecular inhibitor of clostripain automaturation

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CLOSTRIPAIN; CORE PROTEIN; PROTEINASE;

EID: 0029911311     PISSN: 03438651     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002849900114     Document Type: Article
Times cited : (15)

References (22)
  • 1
    • 0028328469 scopus 로고
    • Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases
    • Allaire M, Chernaia MM, Malcolm BA, James MNG (1994) Picornaviral 3C cysteine proteinases have a fold similar to chymotrypsin-like serine proteinases. Nature 369:72-76
    • (1994) Nature , vol.369 , pp. 72-76
    • Allaire, M.1    Chernaia, M.M.2    Malcolm, B.A.3    James, M.N.G.4
  • 2
    • 0019948262 scopus 로고
    • L-trans-epoxysuccinyl-leucylamido (4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L
    • Barrett AJ, Kembhavi AA, Brown MA, Kirschke H, Knight CG, Tamai M, Hanada K (1982) L-trans-epoxysuccinyl-leucylamido (4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem J 201:189-198
    • (1982) Biochem J , vol.201 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3    Kirschke, H.4    Knight, C.G.5    Tamai, M.6    Hanada, K.7
  • 3
    • 0000686943 scopus 로고
    • Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: Structural and functional implications
    • Bazan JF, Fletterick RJ (1988) Viral cysteine proteases are homologous to the trypsin-like family of serine proteases: structural and functional implications. Proc Natl Acad Sci USA 85:7872-7876
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7872-7876
    • Bazan, J.F.1    Fletterick, R.J.2
  • 4
    • 0028923541 scopus 로고
    • Alignment/phylogeny of the papain superfamily of cysteine proteases
    • Berti PJ, Storer AC (1995) Alignment/phylogeny of the papain superfamily of cysteine proteases. J Mol Biol 246:273-283
    • (1995) J Mol Biol , vol.246 , pp. 273-283
    • Berti, P.J.1    Storer, A.C.2
  • 5
    • 0343791122 scopus 로고
    • Proteases in protein maturation
    • Beynon RJ, Bond JS (eds) IRL Press, Oxford
    • Birch NP, Peng Loh Y (1989) Proteases in protein maturation. In: Beynon RJ, Bond JS (eds) Proteolytic enzymes - a practical approach. IRL Press, Oxford, pp 211-230
    • (1989) Proteolytic Enzymes - A Practical Approach , pp. 211-230
    • Birch, N.P.1    Peng Loh, Y.2
  • 6
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock WO, Fernandez JM, Short JM (1987) XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. Biotechniques 5:376-379
    • (1987) Biotechniques , vol.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 7
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou PY, Fasman GD (1978a) Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol 47:45-148
    • (1978) Adv Enzymol , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 8
    • 0017868338 scopus 로고
    • Empirical prediction of protein conformation
    • Chou PY, Fasman GD (1978b) Empirical prediction of protein conformation. Annu Rev Biochem 47:251-276
    • (1978) Annu Rev Biochem , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 9
    • 0027244427 scopus 로고
    • The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene
    • Dargatz H, Diefenthal T, Witte V, Reipen G, von Wettstein D (1993) The heterodimeric protease clostripain from Clostridium histolyticum is encoded by a single gene. Mol Gen Genet 240:140-145
    • (1993) Mol Gen Genet , vol.240 , pp. 140-145
    • Dargatz, H.1    Diefenthal, T.2    Witte, V.3    Reipen, G.4    Von Wettstein, D.5
  • 10
    • 0018786290 scopus 로고
    • α-Clostripain: Chemical characterization, activity, and thiol content of the highly active form of clostripain
    • Gilles AM, Imhoff JM, Keil B (1979) α-Clostripain: chemical characterization, activity, and thiol content of the highly active form of clostripain. J Biol Chem 254:1462-1468
    • (1979) J Biol Chem , vol.254 , pp. 1462-1468
    • Gilles, A.M.1    Imhoff, J.M.2    Keil, B.3
  • 11
    • 0021103445 scopus 로고
    • Amino-acid sequences of the active-site sulfhydryl peptide and other thiol peptides from the cysteine proteinase α-dostripain
    • Gilles AM, De Wolf A, Keil B (1983) Amino-acid sequences of the active-site sulfhydryl peptide and other thiol peptides from the cysteine proteinase α-dostripain. Eur J Biochem 130:473-479
    • (1983) Eur J Biochem , vol.130 , pp. 473-479
    • Gilles, A.M.1    De Wolf, A.2    Keil, B.3
  • 12
    • 0021769432 scopus 로고
    • Evidence for an active-center cysteine in the SH-proteinase α-clostripain through use of N-tosyl-L-lysin chloromethyl ketone
    • Gilles AM, Keil B (1984) Evidence for an active-center cysteine in the SH-proteinase α-clostripain through use of N-tosyl-L-lysin chloromethyl ketone. FEBS Lett 173:58-62
    • (1984) FEBS Lett , vol.173 , pp. 58-62
    • Gilles, A.M.1    Keil, B.2
  • 13
    • 0024495898 scopus 로고
    • Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases: A distinct protein superfamily with a common structural fold
    • Gorbalenya AE, Donchenko AP, Blinov VM, Koomin EV (1989) Cysteine proteases of positive strand RNA viruses and chymotrypsin-like serine proteases: a distinct protein superfamily with a common structural fold. FEBS Lett 243:103-114
    • (1989) FEBS Lett , vol.243 , pp. 103-114
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Blinov, V.M.3    Koomin, E.V.4
  • 15
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton RM, Hunt HD, Ho SN, Pullern JK, Pease L (1989) Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 77:61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullern, J.K.4    Pease, L.5
  • 16
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 17
    • 0027416762 scopus 로고
    • Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: Evidence of a functional relationship with trypsin-like serine proteinases
    • Miyashita K, Kusumi M, Utsumi R, Katayama S, Noda M, Komano T, Satoh N (1993) Site-directed mutagenesis of the putative active site residues of 3C proteinase of coxsackievirus B3: evidence of a functional relationship with trypsin-like serine proteinases. Prot Eng 6:189-193
    • (1993) Prot Eng , vol.6 , pp. 189-193
    • Miyashita, K.1    Kusumi, M.2    Utsumi, R.3    Katayama, S.4    Noda, M.5    Komano, T.6    Satoh, N.7
  • 18
    • 0001571153 scopus 로고
    • The diversity of proteolytic enzymes
    • Beynon RJ, Bond JS (eds) IRL Press, Oxford
    • Neurath H (1989) The diversity of proteolytic enzymes. In: Beynon RJ, Bond JS (eds) Proteolytic enzymes - a practical approach. IRL Press, Oxford, pp 1-13
    • (1989) Proteolytic Enzymes - A Practical Approach , pp. 1-13
    • Neurath, H.1
  • 19
    • 0017798828 scopus 로고
    • Prediction of chain turns in globular proteins on a hydrophobic basis
    • Rose GD (1978) Prediction of chain turns in globular proteins on a hydrophobic basis. Nature 272:586-590
    • (1978) Nature , vol.272 , pp. 586-590
    • Rose, G.D.1
  • 21
    • 0024828408 scopus 로고
    • Secretion, processing and activation of bacterial extracellular proteases
    • Wandersman C (1989) Secretion, processing and activation of bacterial extracellular proteases. Mol Microbiol 3:1825-1831
    • (1989) Mol Microbiol , vol.3 , pp. 1825-1831
    • Wandersman, C.1
  • 22
    • 0028244130 scopus 로고
    • Heterologous expression of the clostripain gene from Clostridium histolyticum in Escherichia coli and Bacillus subtilis: Maturation of the clostripain precursor is coupled with self-activation
    • Witte V, Wolf N, Diefenthal T, Reipen G, Dargatz H (1994) Heterologous expression of the clostripain gene from Clostridium histolyticum in Escherichia coli and Bacillus subtilis: maturation of the clostripain precursor is coupled with self-activation. Microbiology 140:1175-1182
    • (1994) Microbiology , vol.140 , pp. 1175-1182
    • Witte, V.1    Wolf, N.2    Diefenthal, T.3    Reipen, G.4    Dargatz, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.