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Volumn 147, Issue 2, 2010, Pages 167-174

Differences in the P1' substrate specificities of pepsin A and chymosin

Author keywords

Aspartic proteinase; Chymosin; Pepsin A; Proteolytic activity; Substrate specificity

Indexed keywords

ASPARTIC PROTEINASE; CHYMOSIN; PEPSIN A;

EID: 76949107198     PISSN: 0021924X     EISSN: 17562651     Source Type: Journal    
DOI: 10.1093/jb/mvp158     Document Type: Article
Times cited : (14)

References (30)
  • 1
    • 0035987666 scopus 로고    scopus 로고
    • A history of pepsin and related enzymes
    • Fruton, J.S. (2002) A history of pepsin and related enzymes. Q. Rev. Biol. 77, 127-147
    • (2002) Q. Rev. Biol. , vol.77 , pp. 127-147
    • Fruton, J.S.1
  • 2
    • 0019743933 scopus 로고
    • Gastric proteinases - Structure, function, evolution and mechanism of action
    • Foltmann, B. (1981) Gastric proteinases - structure, function, evolution and mechanism of action. Essays Biochem. 17, 52-84
    • (1981) Essays Biochem. , vol.17 , pp. 52-84
    • Foltmann, B.1
  • 3
    • 0036181085 scopus 로고    scopus 로고
    • Pepsinogens, progastricsins, and prochymosins: Structure, function, evolution, and development
    • Kageyama, T. (2002) Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development. Cell. Mol. Life Sci. 59, 288-306
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 288-306
    • Kageyama, T.1
  • 4
    • 0000232655 scopus 로고
    • Prochymosin and chymosin
    • Foltmann, B. (1970) Prochymosin and chymosin. Methods Enzymol. 19, 421-436
    • (1970) Methods Enzymol. , vol.19 , pp. 421-436
    • Foltmann, B.1
  • 5
    • 0026497631 scopus 로고
    • Chymosin: A short review on foetal and neonatal gastric proteases
    • Foltmann, B. (1992) Chymosin: a short review on foetal and neonatal gastric proteases. Scand. J. Clin. Lab. Invest. 52 (Suppl 210), 65-79
    • (1992) Scand. J. Clin. Lab. Invest. , vol.52 , Issue.SUPPL. 210 , pp. 65-79
    • Foltmann, B.1
  • 6
    • 0025290527 scopus 로고
    • The structure and function of the aspartic proteinases
    • Davies, D.R. (1990) The structure and function of the aspartic proteinases. Annu. Rev. Biophys. Biophys. Chem. 19, 189-215
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 189-215
    • Davies, D.R.1
  • 7
    • 0036882390 scopus 로고    scopus 로고
    • Structure and mechanism of the pepsin-like family of aspartic peptidases
    • Dunn, B.M. (2002) Structure and mechanism of the pepsin-like family of aspartic peptiDases. Chem. Rev. 102, 4431-4458
    • (2002) Chem. Rev. , vol.102 , pp. 4431-4458
    • Dunn, B.M.1
  • 8
    • 0014723020 scopus 로고
    • The specificity and mechanism of pepsin action
    • Fruton, J.S. (1970) The specificity and mechanism of pepsin action. Adv. Enzymol. Relat. Areas Mol. Biol. 33, 401-443
    • (1970) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.33 , pp. 401-443
    • Fruton, J.S.1
  • 10
    • 2442671800 scopus 로고
    • Studies on the extended active sites of acid proteinases
    • Sampath-Kumar, P.S. and Fruton, J.S. (1974) Studies on the extended active sites of acid proteinases. Proc. Natl Acad. Sci. USA 71, 1070-1072
    • (1974) Proc. Natl Acad. Sci. USA , vol.71 , pp. 1070-1072
    • Sampath-Kumar, P.S.1    Fruton, J.S.2
  • 11
    • 0025752398 scopus 로고
    • Hydrolysis of beta-casein by gastric proteases. I. Comparison of proteolytic action of bovine chymosin and pepsin A
    • Guillou, H., Miranda, G., and Pelissier, J.P. (1991) Hydrolysis of beta-casein by gastric proteases. I. Comparison of proteolytic action of bovine chymosin and pepsin A. Int. J. Pept. Protein Res. 37, 494-501
    • (1991) Int. J. Pept. Protein Res. , vol.37 , pp. 494-501
    • Guillou, H.1    Miranda, G.2    Pelissier, J.P.3
  • 13
    • 0032078832 scopus 로고    scopus 로고
    • Proteolytic specificity of chymosin on caprine alpha s1-caseins A and F
    • Trujillo, A.J., Miranda, G., Lebars, D., and Delacroix- Buchet, A. (1998) Proteolytic specificity of chymosin on caprine alpha s1-caseins A and F. J. Dairy Res. 65, 233-241
    • (1998) J. Dairy Res. , vol.65 , pp. 233-241
    • Trujillo, A.J.1    Miranda, G.2    Lebars, D.3    Delacroix- Buchet, A.4
  • 14
    • 0022766162 scopus 로고
    • A systematic series of synthetic chromophoric substrates for aspartic proteinases
    • Dunn, B.M., Jimenez, M., Parten, B.F., Valler, M.J., Rolph, C.E., and Kay, J. (1986) A systematic series of synthetic chromophoric substrates for aspartic proteinases. Biochem. J. 237, 899-906
    • (1986) Biochem. J. , vol.237 , pp. 899-906
    • Dunn, B.M.1    Jimenez, M.2    Parten, B.F.3    Valler, M.J.4    Rolph, C.E.5    Kay, J.6
  • 15
    • 0023190117 scopus 로고
    • The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: Evidence for specific interactions in subsites S3 and S2
    • Dunn, B.M., Valler, M.J., Rolph, C.E., Foundling, S.I., Jimenez, M., and Kay, J. (1987) The pH dependence of the hydrolysis of chromogenic substrates of the type, Lys-Pro-Xaa-Yaa-Phe-(NO2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2. Biochim. Biophys. Acta. 913, 122-130
    • (1987) Biochim. Biophys. Acta. , vol.913 , pp. 122-130
    • Dunn, B.M.1    Valler, M.J.2    Rolph, C.E.3    Foundling, S.I.4    Jimenez, M.5    Kay, J.6
  • 16
    • 0034615552 scopus 로고    scopus 로고
    • The two sides of enzyme-substrate specificity: Lessons from the aspartic proteinases
    • Dunn, B.M. and Hung, S. (2000) The two sides of enzyme-substrate specificity: lessons from the aspartic proteinases. Biochim. Biophys. Acta 1477, 231-240
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 231-240
    • Dunn, B.M.1    Hung, S.2
  • 17
    • 0029071169 scopus 로고
    • Processing of the precursors to neurotensin and other bioactive peptides by cathepsin e
    • Kageyama, T., Ichinose, M., and Yonezawa, S. (1995) Processing of the precursors to neurotensin and other bioactive peptides by cathepsin E. J. Biol. Chem. 270, 19135-19140
    • (1995) J. Biol. Chem. , vol.270 , pp. 19135-19140
    • Kageyama, T.1    Ichinose, M.2    Yonezawa, S.3
  • 18
    • 10044263144 scopus 로고    scopus 로고
    • Role of S'1 loop residues in the substrate specificities of pepsin A and chymosin
    • Kageyama, T. (2004) Role of S'1 loop residues in the substrate specificities of pepsin A and chymosin. Biochemistry. 43, 15122-15130
    • (2004) Biochemistry. , vol.43 , pp. 15122-15130
    • Kageyama, T.1
  • 19
    • 52349108761 scopus 로고
    • The estimation of pepsin with hemoglobin
    • Anson, M.L. and Mirsky, A.E. (1932) The estimation of pepsin with hemoglobin. J. Gen. Physiol. 16, 59-63
    • (1932) J. Gen. Physiol. , vol.16 , pp. 59-63
    • Anson, M.L.1    Mirsky, A.E.2
  • 21
    • 0023153985 scopus 로고
    • Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes
    • Stephenson, S.L. and Kenny, A.J. (1987) Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes. Biochem. J. 241, 237-247
    • (1987) Biochem. J. , vol.241 , pp. 237-247
    • Stephenson, S.L.1    Kenny, A.J.2
  • 22
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 23
    • 0004262303 scopus 로고
    • 3rd edn, Longman Group Ltd., London
    • Dixon, M. and Webb, E.C. (1979) Enzymes. 3rd edn, pp. 332-467, Longman Group Ltd., London
    • (1979) Enzymes , pp. 332-467
    • Dixon, M.1    Webb, E.C.2
  • 25
    • 0021215080 scopus 로고
    • Structure of ethanol-inhibited porcine pepsin at 2-A? resolution and binding of the methyl ester of phenylalanyl-diiodotyrosine to the enzyme
    • Andreeva, N.S., ZDanov, A.S., Gustchina, A.E., and Fedorov, A.A. (1984) Structure of ethanol-inhibited porcine pepsin at 2-A? resolution and binding of the methyl ester of phenylalanyl-diiodotyrosine to the enzyme. J. Biol. Chem. 259, 11353-11365
    • (1984) J. Biol. Chem. , vol.259 , pp. 11353-11365
    • Andreeva, N.S.1    Zdanov, A.S.2    Gustchina, A.E.3    Fedorov, A.A.4
  • 26
    • 0025297753 scopus 로고
    • X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3A ? resolution
    • Cooper, J.B., Khan, G., Taylor, G., Tickle, J.I., and Blundell, T.L. (1990) X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3A ? resolution. J. Mol. Biol. 214, 199-222
    • (1990) J. Mol. Biol. , vol.214 , pp. 199-222
    • Cooper, J.B.1    Khan, G.2    Taylor, G.3    Tickle, J.I.4    Blundell, T.L.5
  • 27
    • 0025354599 scopus 로고
    • Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8A ? resolution
    • Sielecki, A.R., Fedorov, A.A., Boodhoo, A., Andreeva, N.S., and James, M.N. (1990) Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8A ? resolution. J. Mol. Biol. 214, 143-170
    • (1990) J. Mol. Biol. , vol.214 , pp. 143-170
    • Sielecki, A.R.1    Fedorov, A.A.2    Boodhoo, A.3    Andreeva, N.S.4    James, M.N.5
  • 28
    • 0025374191 scopus 로고
    • The three-dimensional structure of recombinant bovine chymosin at 2.3A ? resolution
    • Gilliland, G.L., Winborne, E.L., Nachman, J., and WloDawer, A. (1990) The three-dimensional structure of recombinant bovine chymosin at 2.3A ? resolution. Proteins 8, 82-101
    • (1990) Proteins , vol.8 , pp. 82-101
    • Gilliland, G.L.1    Winborne, E.L.2    Nachman, J.3    Wlo Dawer, A.4
  • 29
    • 0025935211 scopus 로고
    • X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2A ? resolution of bovine chymosin
    • Newman, M., Safro, M., Frazao, C., Khan, G., ZDanov, A., Tickle, J.I., Blundell, T.L., and Andreeva, N. (1991) X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2A ? resolution of bovine chymosin. J. Mol. Biol. 221, 1295-1309
    • (1991) J. Mol. Biol. , vol.221 , pp. 1295-1309
    • Newman, M.1    Safro, M.2    Frazao, C.3    Khan, G.4    Zdanov, A.5    Tickle, J.I.6    Blundell, T.L.7    Andreeva, N.8
  • 30
    • 0034736285 scopus 로고    scopus 로고
    • Psychrophilic enzymes: Revisiting the thermodynamic parameters of activation may explain local flexibility
    • Lonhienne, T., Gerday, C., and Feller, G. (2000) Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility. Biochim. Biophys. Acta 1543, 1-10
    • (2000) Biochim. Biophys. Acta , vol.1543 , pp. 1-10
    • Lonhienne, T.1    Gerday, C.2    Feller, G.3


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