메뉴 건너뛰기




Volumn 1477, Issue 1-2, 2000, Pages 231-240

The two sides of enzyme-substrate specificity: Lessons from the aspartic proteinases

Author keywords

Aspartic proteinase; Chromogenic substrate; Enzyme active site; Enzyme kinetics; Mutagenesis of active site residues; Substrate specificity

Indexed keywords

ASPARTIC PROTEINASE;

EID: 0034615552     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00275-7     Document Type: Review
Times cited : (64)

References (31)
  • 1
    • 0014220925 scopus 로고
    • Evolution of structure and function of proteases
    • Neurath H., Walsh K.A., Winter W.P. Evolution of structure and function of proteases. Science. 158:1967;1638-1644.
    • (1967) Science , vol.158 , pp. 1638-1644
    • Neurath, H.1    Walsh, K.A.2    Winter, W.P.3
  • 2
    • 85025401314 scopus 로고
    • Crystalline pepsin. I. Isolation and tests of purity
    • Northrop J.H. Crystalline pepsin. I. Isolation and tests of purity. J. Gen. Physiol. 13:1930;739-766.
    • (1930) J. Gen. Physiol. , vol.13 , pp. 739-766
    • Northrop, J.H.1
  • 6
    • 0017581877 scopus 로고
    • Penicillopepsin from Penicillium janthinellum crystal structue at 2.8 Å and sequence homology with porcine pepsin
    • Hsu I.N., Delbaere L.T.J., James M.N.G., Hofmann T. Penicillopepsin from Penicillium janthinellum crystal structue at 2.8 Å and sequence homology with porcine pepsin. Nature. 266:1983;140-145.
    • (1983) Nature , vol.266 , pp. 140-145
    • Hsu, I.N.1    Delbaere, L.T.J.2    James, M.N.G.3    Hofmann, T.4
  • 8
    • 77956987576 scopus 로고
    • Techniques in enzymic hydrolysis
    • Smyth D.G. Techniques in enzymic hydrolysis. Methods Enzymol. XI:1967;214-231.
    • (1967) Methods Enzymol. , vol.11 , pp. 214-231
    • Smyth, D.G.1
  • 9
    • 0014599704 scopus 로고
    • Pyridyl esters of peptides as synthetic substrates of pepsin
    • Sachdev G.P., Fruton J.S. Pyridyl esters of peptides as synthetic substrates of pepsin. Biochemistry. 8:1969;4231-4238.
    • (1969) Biochemistry , vol.8 , pp. 4231-4238
    • Sachdev, G.P.1    Fruton, J.S.2
  • 11
    • 0014352493 scopus 로고
    • The substrate specificity of pepsin C
    • Ryle A.P., Leclerc J., Falla F. The substrate specificity of pepsin C. Biochem. J. 110:1968;p4.
    • (1968) Biochem. J. , vol.110 , pp. 4
    • Ryle, A.P.1    Leclerc, J.2    Falla, F.3
  • 12
    • 0017676727 scopus 로고
    • Specificity and mechanism of pepsin action on synthetic substrates
    • Fruton J.S. Specificity and mechanism of pepsin action on synthetic substrates. Adv. Exp. Med. Biol. 95:1977;131-140.
    • (1977) Adv. Exp. Med. Biol. , vol.95 , pp. 131-140
    • Fruton, J.S.1
  • 14
    • 0020144910 scopus 로고
    • A new chromogenic substrate for penicillopepsin and other fungal aspartic proteinases
    • Hofmann T., Hodges R.S. A new chromogenic substrate for penicillopepsin and other fungal aspartic proteinases. Biochem. J. 203:1982;603-610.
    • (1982) Biochem. J. , vol.203 , pp. 603-610
    • Hofmann, T.1    Hodges, R.S.2
  • 15
    • 0021415850 scopus 로고    scopus 로고
    • The synthesis, purification, and evaluation of a new chromophoric substrate for pepsin and other aspartyl proteases
    • Dunn B.M., Kammermann B., McCurry K.R. The synthesis, purification, and evaluation of a new chromophoric substrate for pepsin and other aspartyl proteases. Anal. Biochem. 138:1084;68-73.
    • Anal. Biochem. , vol.138 , pp. 68-73
    • Dunn, B.M.1    Kammermann, B.2    McCurry, K.R.3
  • 16
    • 0022766162 scopus 로고
    • A systematic series of synthetic chromogenic substrates for aspartic proteinases
    • Dunn B.M., Jimenez M., Parten B.F., Valler M.J., Rolph C.E., Kay J. A systematic series of synthetic chromogenic substrates for aspartic proteinases. Biochem. J. 237:1986;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
  • 17
    • 0024298841 scopus 로고
    • Secondary enzyme-substrate interactions use of kinetic evidence for ionic interaction between substrate side chains and the pepsin active site
    • Pohl J., Dunn B.M. Secondary enzyme-substrate interactions use of kinetic evidence for ionic interaction between substrate side chains and the pepsin active site. Biochemistry. 27:1988;4827-4834.
    • (1988) Biochemistry , vol.27 , pp. 4827-4834
    • Pohl, J.1    Dunn, B.M.2
  • 19
    • 0343831693 scopus 로고    scopus 로고
    • The promiscuous active site specificity/binding preferences of the fungal aspartic proteinase, Rhizopuspepsin
    • Lowther W.T., Dunn B.M. The promiscuous active site specificity/binding preferences of the fungal aspartic proteinase, Rhizopuspepsin. Protein Peptide Lett. 5:1998;303-316.
    • (1998) Protein Peptide Lett. , vol.5 , pp. 303-316
    • Lowther, W.T.1    Dunn, B.M.2
  • 20
    • 0027400775 scopus 로고
    • Exploration of subsite binding specificity of human cathepsin D through kinetics and knowledge-based molecular modeling
    • Scarborough P.E., Guruprasad K., Blundell T.L., Richo G.R., Conner G.E., Dunn B.M. Exploration of subsite binding specificity of human cathepsin D through kinetics and knowledge-based molecular modeling. Protein Sci. 2:1993;264-276.
    • (1993) Protein Sci. , vol.2 , pp. 264-276
    • Scarborough, P.E.1    Guruprasad, K.2    Blundell, T.L.3    Richo, G.R.4    Conner, G.E.5    Dunn, B.M.6
  • 22
    • 0031952604 scopus 로고    scopus 로고
    • Prime region subsite specificity characterizaion of human cathepsin D. The dominant role of position 128
    • Beyer B.M., Dunn B.M. Prime region subsite specificity characterizaion of human cathepsin D. The dominant role of position 128. Protein Sci. 7:1997;88-95.
    • (1997) Protein Sci. , vol.7 , pp. 88-95
    • Beyer, B.M.1    Dunn, B.M.2
  • 28
    • 0032478123 scopus 로고    scopus 로고
    • Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p) enhanced for substrates with arginine residues flanking the P1 site: Correlation with electronegative active site pockets predicted by molecular modeling
    • Olsen V., Guruprasad K., Cawley N.X., Chen H.-C., Blundell T.L., Loh Y.P. Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p) enhanced for substrates with arginine residues flanking the P1 site: correlation with electronegative active site pockets predicted by molecular modeling. Biochemistry. 37:1998;2768-2777.
    • (1998) Biochemistry , vol.37 , pp. 2768-2777
    • Olsen, V.1    Guruprasad, K.2    Cawley, N.X.3    Chen, H.-C.4    Blundell, T.L.5    Loh, Y.P.6
  • 31
    • 0032538544 scopus 로고    scopus 로고
    • The enhancing of a cysteine proteinase activity at acidic pH by protein engineering, the role of glutamic 50 in the enzyme mechanism of caricain
    • Ikeuchi Y., Katerelos N.A., Goodenough P.W. The enhancing of a cysteine proteinase activity at acidic pH by protein engineering, the role of glutamic 50 in the enzyme mechanism of caricain. FEBS Lett. 437:1998;91-96.
    • (1998) FEBS Lett. , vol.437 , pp. 91-96
    • Ikeuchi, Y.1    Katerelos, N.A.2    Goodenough, P.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.