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1
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0003755878
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Aspartic Proteinases and Their Inhibitors
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Walter de Grayer: Berlin (b) Tang, J., Ed. Acid Proteinases, Structure, Function, and Biology; Plenum: New York, 1977; p 95. (c) Fersht, A. Enzyme Structure and Mechanism; W. H. Freeman: New York, 1985; pp 422–426. (d) Fruton, J. P. Adv. Enzymol. Relat. Areas Mol Biol. 1976, 44, 1–36. (e) Polgár, L. FEBS Lett. 1987, 219, 1–4
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(a) Aspartic Proteinases and Their Inhibitors; Proceedings of FEBS Advanced Course No. 84/07; Kosta, V., Ed.; Walter de Grayer: Berlin, 1985. (b) Tang, J., Ed. Acid Proteinases, Structure, Function, and Biology; Plenum: New York, 1977; p 95. (c) Fersht, A. Enzyme Structure and Mechanism; W. H. Freeman: New York, 1985; pp 422–426. (d) Fruton, J. P. Adv. Enzymol. Relat. Areas Mol Biol. 1976, 44, 1–36. (e) Polgár, L. FEBS Lett. 1987, 219, 1–4.
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Proceedings of FEBS Advanced Course No. 84/07
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Kosta, V.1
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2
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0017581877
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Subramanian, E.; Swan, I. D. A.; Liu, M.; Davies, D. R.; Jenkins, J. A.; Tickle, I. J.; Blundell, T. L. Proc. Natl. Acad. Sci. U.S.A. 1977, 74, 556–559. (c) Jenkins, J. A.; Tickle, I. J.; Sewell, T.; Ungaretti, J.; Wollmer, A.; Blundell, T. In Acid Proteases, Structure, Function and Biology; Tang, J., Ed.; Plenum: New York, 1977; pp 43–60. (d) Andreeva, N. S.; Zdanov, A. S.; Gustchina, A. E.; Fedorov, A. A. J. Biol. Chem. 1984, 259, 11353–11365. (e) Bott, R.; Subramanian, E.; Davies, D. R. Biochemistry 1982, 21, 6956–6962. (f) James, M. N. G.; Sielecki, A. R. Biochemistry 1985, 24, 3701–3713 and references therein
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(a) Hsu, I.-N.; Delbaere, L. T. J.; James, M. N. G.; Hofmann, T. Nature (London) 1977, 266, 140–145. (b) Subramanian, E.; Swan, I. D. A.; Liu, M.; Davies, D. R.; Jenkins, J. A.; Tickle, I. J.; Blundell, T. L. Proc. Natl. Acad. Sci. U.S.A. 1977, 74, 556–559. (c) Jenkins, J. A.; Tickle, I. J.; Sewell, T.; Ungaretti, J.; Wollmer, A.; Blundell, T. In Acid Proteases, Structure, Function and Biology; Tang, J., Ed.; Plenum: New York, 1977; pp 43–60. (d) Andreeva, N. S.; Zdanov, A. S.; Gustchina, A. E.; Fedorov, A. A. J. Biol. Chem. 1984, 259, 11353–11365. (e) Bott, R.; Subramanian, E.; Davies, D. R. Biochemistry 1982, 21, 6956–6962. (f) James, M. N. G.; Sielecki, A. R. Biochemistry 1985, 24, 3701–3713 and references therein.
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Nature (London)
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Hsu, I.-N.1
Delbaere, L.T.J.2
James, M.N.G.3
Hofmann, T.4
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3
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85022258995
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For a review on the current status of thinking on the mechanism, see: Appendix of
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For a review on the current status of thinking on the mechanism, see: Appendix of Hofmann, T.; Dunn, B. M.; Fink, A. L. in ref 4a.
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ref 4a
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Hofmann, T.1
Dunn, B.M.2
Fink, A.L.3
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4
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0021769546
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Dunn, B. M.; Fink, A. L. Biochemistry 1984, 23, 5231–5247
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(a) Hofmann, T.; Fink, A. L. Biochemistry 1984, 23, 5247–5256. (b) Dunn, B. M.; Fink, A. L. Biochemistry 1984, 23, 5231–5247.
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Biochemistry
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Hofmann, T.1
Fink, A.L.2
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6
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37049123599
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Kirby, A. J.; McDonald, R. S.; Smith, C. R. J. Chem. Soc., Perkin Trans. 2 1984, 1495–1504
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(a) Aldersley, M. F.; Kirby, A. J.; Lancaster, P. W.; McDonald, R. S.; Smith, C. R. J. Chem. Soc., Perkin Trans. 2 1974, 1487–1495. (b) Kirby, A. J.; McDonald, R. S.; Smith, C. R. J. Chem. Soc., Perkin Trans. 2 1984, 1495–1504.
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Aldersley, M.F.1
Kirby, A.J.2
Lancaster, P.W.3
McDonald, R.S.4
Smith, C.R.5
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8
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Holladay, M. W.; Salituro, F. G.; Schmidt, P. G.; Rich, D. H. Biochem. Soc. Trans. 1985, 13, 1046–1048
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(a) Antonov, V. K.; Ginodman, L. M.; Kapitannikov, Yu. V.; Barsheoskaya, T. N.; Gurova, A. G.; Rumsh, L. D. FEBS Lett. 1978, 88, 87–90. (b) Holladay, M. W.; Salituro, F. G.; Schmidt, P. G.; Rich, D. H. Biochem. Soc. Trans. 1985, 13, 1046–1048.
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FEBS Lett.
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Antonov, V.K.1
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Gurova, A.G.5
Rumsh, L.D.6
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9
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0022376670
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Transpeptidation studies that are interpreted in terms of intermediates being generated and held by the enzyme long enough for a second substrate to be bound and peptide reformation to occur have been reported This same possibility has been suggested by Kluger and Chin. Such intermediates may indeed by bound but not necessarily covalently linked to the enzymes at all times
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Transpeptidation studies that are interpreted in terms of intermediates being generated and held by the enzyme long enough for a second substrate to be bound and peptide reformation to occur have been reported: Blum, M.; Cunningham, A.; Bendiver, M.; Hofmann, T. Biochem. Soc. Trans. 1985, 13, 1044–1046. This same possibility has been suggested by Kluger and Chin. Such intermediates may indeed by bound but not necessarily covalently linked to the enzymes at all times.
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Biochem. Soc. Trans.
, vol.13
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Blum, M.1
Cunningham, A.2
Bendiver, M.3
Hofmann, T.4
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11
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0011222187
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Somayaji, V.; Brown, R. S. J. Am. Chem. Soc. 1987, 109, 4738–4739
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(a) Skorey, K. I.; Somayaji, V.; Brown, R. S.; Ball, R. G. J. Org. Chem. 1986, 51, 4866–4872, (b) Somayaji, V.; Brown, R. S. J. Am. Chem. Soc. 1987, 109, 4738–4739.
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Guthrie, P. J. J. Am. chem. Soc. 1974, 96, 3608–3615. (c) Arnett, E. M.; Quirk, R. P.; Larsen, J. W. J. Am. Chem. Soc. 1970, 92, 3977–3984
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(a) Arnett, E. M. Prog. Phys. Org. Chem. 1963, 1, 223–403. (b) Guthrie, P. J. J. Am. chem. Soc. 1974, 96, 3608–3615. (c) Arnett, E. M.; Quirk, R. P.; Larsen, J. W. J. Am. Chem. Soc. 1970, 92, 3977–3984.
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Arnett, E.M.1
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Malonic anhydride has been synthesized by the ozonolysis of ketene dimer, but that is unstable above -30 °C: Perrin, C. L.; Arrhenius, T. J. Am. Chem. Soc. 1978, 100, 5249–5151
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(a) Kirby, A. J. Adv. Phys. Org. Chem. 1980, 17, 183–278. (b) Malonic anhydride has been synthesized by the ozonolysis of ketene dimer, but that is unstable above -30 °C: Perrin, C. L.; Arrhenius, T. J. Am. Chem. Soc. 1978, 100, 5249–5151.
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Medzihradszky, K.; Voynick, I. M.; Medzihradszky-Schweiger, M.; Fruton, J. S. Biochemistry 1970, 9, 1154–1162. (c) Pearl, L. in ref la, pp 189–195
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(a) Sachdev, G. P.; Fruton, J. S. Proc. Natl. Acad. Sci. U.S.A. 1975, 72, 3424–3427. (b) Medzihradszky, K.; Voynick, I. M.; Medzihradszky-Schweiger, M.; Fruton, J. S. Biochemistry 1970, 9, 1154–1162. (c) Pearl, L. in ref la, pp 189–195.
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Sachdev, G.P.1
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0003481596
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For discussion of the pros and cons of enzyme binding inducing significant substrate strain or stress, see 2nd ed.; W. H. Freeman: San Francisco (b) Jencks, W. P. Adv. Enzymol. Relat. Areas Mol. Biol. 1975, 43, 219-410; 1980, 51, 75–106. (c) Palcic, M. M.; Klinman, J. P. Biochemistry 1983, 22, 5957–5966 and references therein
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For discussion of the pros and cons of enzyme binding inducing significant substrate strain or stress, see: (a) Fersht, A. R. Enzyme Structure and Mechanism, 2nd ed.; W. H. Freeman: San Francisco, 1985; pp 311–346. (b) Jencks, W. P. Adv. Enzymol. Relat. Areas Mol. Biol. 1975, 43, 219-410; 1980, 51, 75–106. (c) Palcic, M. M.; Klinman, J. P. Biochemistry 1983, 22, 5957–5966 and references therein.
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Enzyme Structure and Mechanism
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Fersht, A.R.1
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20
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0006371410
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Accelerated hydrolysis of amides due to N-pyramidalization has been studied
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Accelerated hydrolysis of amides due to N-pyramidalization has been studied: Ślebocka-Tilk, H.; Brown, R. S. J. Org. Chem. 1987, 52, 805–808.
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J. Org. Chem.
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Wang, T. T.; Hofmann, T. Biochem. J. 1976, 153, 691–699
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(a) Takahashi, M.; Wang, T. T.; Hofmann, T. Biochem. Biophys. Res. Commun. 1974, 57, 39–46. (b) Wang, T. T.; Hofmann, T. Biochem. J. 1976, 153, 691–699.
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Antonov, V. K. in ref la, pp 202–220
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(a) Antonov, V. K.; Ginodman, L. M.; Rumsh, L. D.; Kapitannikov, Yu. V.; Barshevskaya, T. N.; Yavashev, L. P.; Gurova, A. G.; Volkova, L. I. Bioorg. Khim. 1980, 6, 436–446. (b) Antonov, V. K. in ref la, pp 202–220.
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Bioorg. Khim.
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Antonov, V.K.1
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Yavashev, L.P.6
Gurova, A.G.7
Volkova, L.I.8
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23
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0019575864
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Antonov, V. K.; Linsdman, L. M.; Rumsh, L. D.; Kapitannikov, Yu. V.; Barshevskaya, T. N.; Yavashev, A. G.; Gurova, A. G.; Volkova, L. I. Eur. J. Biochem. 1981, 117, 195–200.
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Eur. J. Biochem.
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Antonov, V.K.1
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Rumsh, L.D.3
Kapitannikov, Y.V.4
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Yavashev, A.G.6
Gurova, A.G.7
Volkova, L.I.8
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