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Volumn 51, Issue 31, 2012, Pages 6164-6170

Importance of tetrahedral intermediate formation in the catalytic mechanism of the serine proteases chymotrypsin and subtilisin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CARBOXYL GROUPS; CARBOXYLATE GROUPS; CATALYTIC EFFICIENCIES; CATALYTIC MECHANISMS; GENERAL BASE; GLYOXAL; HYDROXYL GROUPS; INTERMEDIATE FORMATION; LOW-BARRIER HYDROGEN BONDS; MOLARITY; OXYANIONS; SERINE PROTEASE; SUBSTRATE BINDING; SUBTILISIN; SUBTILISIN CARLSBERG; TETRAHEDRAL INTERMEDIATES;

EID: 84864684042     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300688k     Document Type: Article
Times cited : (15)

References (48)
  • 1
    • 0009738251 scopus 로고
    • The identification of the histidine residue at the active centre of chymotrypsin
    • Ong, E. B., Shaw, E., and Schoellmann, G. (1965) The identification of the histidine residue at the active centre of chymotrypsin J. Biol. Chem. 240, 694-698
    • (1965) J. Biol. Chem. , vol.240 , pp. 694-698
    • Ong, E.B.1    Shaw, E.2    Schoellmann, G.3
  • 2
    • 0002437303 scopus 로고
    • Serine phosphoric acid from diisopropylphosphoryl chymotrypsin
    • Schaffer, N. K., May, S. C., Jr., and Summerson, W. H. (1953) Serine phosphoric acid from diisopropylphosphoryl chymotrypsin J. Biol. Chem. 202, 67-76
    • (1953) J. Biol. Chem. , vol.202 , pp. 67-76
    • Schaffer, N.K.1    May, Jr.S.C.2    Summerson, W.H.3
  • 3
    • 0001244705 scopus 로고
    • Direct evidence for the presence of histidine in the active centre of chymotrypsin
    • Schoellmann, G. and Shaw, E. (1963) Direct evidence for the presence of histidine in the active centre of chymotrypsin Biochemistry 2, 252-255
    • (1963) Biochemistry , vol.2 , pp. 252-255
    • Schoellmann, G.1    Shaw, E.2
  • 4
    • 0014689979 scopus 로고
    • Role of a buried acid group in the mechanism of action of chymotrypsin
    • Blow, D. M., Birktoft, J. J., and Hartley, B. S. (1969) Role of a buried acid group in the mechanism of action of chymotrypsin Nature 221, 337-340
    • (1969) Nature , vol.221 , pp. 337-340
    • Blow, D.M.1    Birktoft, J.J.2    Hartley, B.S.3
  • 5
    • 0001599898 scopus 로고
    • The Reaction of p-nitrophenyl Esters with Chymotrypsin and Insulin
    • Hartley, B. S. and Kilby, B. A. (1954) The Reaction of p-nitrophenyl Esters with Chymotrypsin and Insulin Biochem. J. 56, 288-297
    • (1954) Biochem. J. , vol.56 , pp. 288-297
    • Hartley, B.S.1    Kilby, B.A.2
  • 6
    • 0016904563 scopus 로고
    • Transition state analog inhibitors and enzyme catalysis
    • Wolfenden, R. (1976) Transition state analog inhibitors and enzyme catalysis Annu. Rev. Biophys. Bioeng. 5, 271-306
    • (1976) Annu. Rev. Biophys. Bioeng. , vol.5 , pp. 271-306
    • Wolfenden, R.1
  • 7
    • 0015922129 scopus 로고
    • Mechanism of Chymotrypsin: Structure, Reactivity, and Nonproductive Binding Relationships
    • Fastrez, J. and Fersht, A. R. (1973) Mechanism of Chymotrypsin: Structure, Reactivity, and Nonproductive Binding Relationships Biochemistry 12, 1067-1074
    • (1973) Biochemistry , vol.12 , pp. 1067-1074
    • Fastrez, J.1    Fersht, A.R.2
  • 8
    • 0036489219 scopus 로고    scopus 로고
    • 13C-NMR study of the inhibition of δ-chymotrypsin by a tripeptide-glyoxal inhibitor
    • 13C-NMR study of the inhibition of δ-chymotrypsin by a tripeptide-glyoxal inhibitor Biochem. J. 362, 339-347
    • (2002) Biochem. J. , vol.362 , pp. 339-347
    • Djurdjevic-Pahl, A.1    Hewage, C.2    Malthouse, J.P.G.3
  • 10
    • 0027302689 scopus 로고
    • Peptide glyoxals: A novel class of inhibitor for serine and cysteine proteinases
    • Walker, B., McCarthy, N., Healy, A., Ye, T., and McKervey, M. A. (1993) Peptide glyoxals: A novel class of inhibitor for serine and cysteine proteinases Biochem. J. 293, 321-323
    • (1993) Biochem. J. , vol.293 , pp. 321-323
    • Walker, B.1    McCarthy, N.2    Healy, A.3    Ye, T.4    McKervey, M.A.5
  • 12
    • 67349182183 scopus 로고    scopus 로고
    • Oxyanion and tetrahedral intermediate stabilization by subtilisin: Detection of a new tetrahedral adduct
    • Howe, N., Rogers, L., Hewage, C., and Malthouse, J. P. G. (2009) Oxyanion and tetrahedral intermediate stabilization by subtilisin: Detection of a new tetrahedral adduct Biochim. Biophys. Acta 1794, 1251-1258
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 1251-1258
    • Howe, N.1    Rogers, L.2    Hewage, C.3    Malthouse, J.P.G.4
  • 14
    • 0021104909 scopus 로고
    • On the stability of tetrahedral intermediates within the active sites of serine and cysteine proteases
    • Fastrez, J. (1983) On the stability of tetrahedral intermediates within the active sites of serine and cysteine proteases Eur. J. Biochem. 135, 339-341
    • (1983) Eur. J. Biochem. , vol.135 , pp. 339-341
    • Fastrez, J.1
  • 15
    • 34250858958 scopus 로고    scopus 로고
    • 1H-NMR studies of oxyanion and tetrahedral intermediate stabilization by the serine proteinases: Optimizing inhibitor warhead specificity and potency by studying the inhibition of the serine proteinases by peptide-derived chloromethane and glyoxal inhibitors
    • 1H-NMR studies of oxyanion and tetrahedral intermediate stabilization by the serine proteinases: Optimizing inhibitor warhead specificity and potency by studying the inhibition of the serine proteinases by peptide-derived chloromethane and glyoxal inhibitors Biochem. Soc. Trans. 35, 566-570
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 566-570
    • Malthouse, J.P.G.1
  • 17
    • 0026744397 scopus 로고
    • A study of the stabilization of tetrahedral adducts by trypsin and δ-chymotrypsin
    • Finucane, M. D. and Malthouse, J. P. G. (1992) A study of the stabilization of tetrahedral adducts by trypsin and δ-chymotrypsin Biochem. J. 286, 889-900
    • (1992) Biochem. J. , vol.286 , pp. 889-900
    • Finucane, M.D.1    Malthouse, J.P.G.2
  • 19
    • 34848920136 scopus 로고    scopus 로고
    • An NMR study of the inhibition of pepsin by glyoxal inhibitors: Mechanism of tetrahedral intermediate stabilization by the aspartyl proteinases
    • Cosgrove, S., Rogers, L., Hewage, C., and Malthouse, J. P. G. (2007) An NMR study of the inhibition of pepsin by glyoxal inhibitors: Mechanism of tetrahedral intermediate stabilization by the aspartyl proteinases Biochemistry 46, 11205-11215
    • (2007) Biochemistry , vol.46 , pp. 11205-11215
    • Cosgrove, S.1    Rogers, L.2    Hewage, C.3    Malthouse, J.P.G.4
  • 20
    • 12044258245 scopus 로고
    • 1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive
    • Carpino, L. A. (1993) 1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive J. Am. Chem. Soc. 115, 4397-4398
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4397-4398
    • Carpino, L.A.1
  • 21
    • 0015916420 scopus 로고
    • Total Synthesis of a Moncyclic Peptide Lactone Antibiotic, Etamycin
    • Sheehan, J. C. and Ledis, S. L. (1973) Total Synthesis of a Moncyclic Peptide Lactone Antibiotic, Etamycin J. Am. Chem. Soc. 95, 875-879
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 875-879
    • Sheehan, J.C.1    Ledis, S.L.2
  • 22
    • 0024477849 scopus 로고
    • 13C-NMR investigation of the ionizations within an inhibitor-α-chymotrypsin complex: Evidence that both α-chymotrypsin and trypsin stabilize a hemiketal oxyanion by similar mechanisms
    • 13C-NMR investigation of the ionizations within an inhibitor-α-chymotrypsin complex: Evidence that both α-chymotrypsin and trypsin stabilize a hemiketal oxyanion by similar mechanisms Biochem. J. 258, 853-859
    • (1989) Biochem. J. , vol.258 , pp. 853-859
    • Finucane, M.D.1    Hudson, E.A.2    Malthouse, J.P.G.3
  • 23
    • 0028942691 scopus 로고
    • A study of the stabilization of the oxyanion of tetrahedral adducts by trypsin, chymotrypsin and subtilisin
    • O'Connell, T. P. and Malthouse, J. P. G. (1995) A study of the stabilization of the oxyanion of tetrahedral adducts by trypsin, chymotrypsin and subtilisin Biochem. J. 307, 353-359
    • (1995) Biochem. J. , vol.307 , pp. 353-359
    • O'Connell, T.P.1    Malthouse, J.P.G.2
  • 24
    • 50549163362 scopus 로고
    • The Preparation and Properties of Two New Chromogenic Substrates of Trypsin
    • Erlanger, B. F., Kokowsky, N., and Cohen, W. (1961) The Preparation and Properties of Two New Chromogenic Substrates of Trypsin Arch. Biochem. Biophys. 95, 271-278
    • (1961) Arch. Biochem. Biophys. , vol.95 , pp. 271-278
    • Erlanger, B.F.1    Kokowsky, N.2    Cohen, W.3
  • 25
    • 33845280649 scopus 로고
    • Hydrolysis of a Peptide Bond in Neutral Water
    • Kahne, D. and Clark Still, W. (1988) Hydrolysis of a Peptide Bond in Neutral Water J. Am. Chem. Soc. 110, 7529-7534
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7529-7534
    • Kahne, D.1    Clark Still, W.2
  • 26
    • 0017164971 scopus 로고
    • The active centers of Streptomyces griseus protease 3, α-chymotrypsin, and elastase: Enzyme-substrate interactions close to the scissile bond
    • Bauer, C. A., Thompson, R. C., and Blout, E. R. (1976) The active centers of Streptomyces griseus protease 3, α-chymotrypsin, and elastase: Enzyme-substrate interactions close to the scissile bond Biochemistry 15, 1296-1299
    • (1976) Biochemistry , vol.15 , pp. 1296-1299
    • Bauer, C.A.1    Thompson, R.C.2    Blout, E.R.3
  • 27
    • 84055211882 scopus 로고    scopus 로고
    • A Greatly Under-Appreciated Fundamental Principle of Physical Organic Chemistry
    • Cox, R. A. (2011) A Greatly Under-Appreciated Fundamental Principle of Physical Organic Chemistry J. Mol. Sci. 12, 8316-8332
    • (2011) J. Mol. Sci. , vol.12 , pp. 8316-8332
    • Cox, R.A.1
  • 28
    • 0023463943 scopus 로고
    • Complex of α-Chymotrypsin and N-Acetyl- l -leucyl- l -phenylalanyl Trifluoromethyl Ketone: Structural Studies with NMR Spectroscopy
    • Liang, T. C. and Abeles, R. H. (1987) Complex of α-Chymotrypsin and N-Acetyl- l -leucyl- l -phenylalanyl Trifluoromethyl Ketone: Structural Studies with NMR Spectroscopy Biochemistry 26, 7603-7608
    • (1987) Biochemistry , vol.26 , pp. 7603-7608
    • Liang, T.C.1    Abeles, R.H.2
  • 30
    • 0014945734 scopus 로고
    • Structure of Crystalline α-Chymotrypsin. IV. The Structure of Indoleacryloyl-α-Chymotrypsin and its Relevance to the Hydrolytic Mechanism of the Enzyme
    • Henderson, R. (1970) Structure of Crystalline α-Chymotrypsin. IV. The Structure of Indoleacryloyl-α-Chymotrypsin and its Relevance to the Hydrolytic Mechanism of the Enzyme J. Mol. Biol. 54, 341-354
    • (1970) J. Mol. Biol. , vol.54 , pp. 341-354
    • Henderson, R.1
  • 31
    • 0017324044 scopus 로고
    • Serine Proteases: Structure and Mechanism of Catalysis
    • Kraut, J. (1977) Serine Proteases: Structure and Mechanism of Catalysis Annu. Rev. Biochem. 46, 331-358
    • (1977) Annu. Rev. Biochem. , vol.46 , pp. 331-358
    • Kraut, J.1
  • 32
    • 33646195474 scopus 로고
    • The hydrogen bond in molecular recognition
    • Fersht, A. R. (1987) The hydrogen bond in molecular recognition Trends Biochem. Sci. 12, 301-304
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 301-304
    • Fersht, A.R.1
  • 34
    • 0000417921 scopus 로고
    • Strongly basic systems. VIII H-function for dimethyl sulfoxide-water- tetramethylammonium hydroxide
    • Dolman, D. and Stewart, R. (1967) Strongly basic systems. VIII. H-function for dimethyl sulfoxide-water-tetramethylammonium hydroxide Can. J. Chem. 45, 911-924
    • (1967) Can. J. Chem. , vol.45 , pp. 911-924
    • Dolman, D.1    Stewart, R.2
  • 35
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W. P. (1981) On the attribution and additivity of binding energies Proc. Natl. Acad. Sci. U.S.A. 78, 4046-4050
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 36
    • 0030759097 scopus 로고    scopus 로고
    • The tortuous story of Asp···His·· ·Ser: Structural analysis of α-chymotrypsin
    • Blow, D. M. (1997) The tortuous story of Asp··· His···Ser: Structural analysis of α-chymotrypsin Trends Biochem. Sci. 22, 405-408
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 405-408
    • Blow, D.M.1
  • 37
    • 79952784475 scopus 로고    scopus 로고
    • The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: A refined mechanism of serine protease action
    • Wahlgren, W. Y., Pal, G., Kardos, J., Porrogi, P., Szenthe, B., Patthy, A., Graf, L., and Katona, G. (2011) The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: A refined mechanism of serine protease action J. Biol. Chem. 286, 3587-3596
    • (2011) J. Biol. Chem. , vol.286 , pp. 3587-3596
    • Wahlgren, W.Y.1    Pal, G.2    Kardos, J.3    Porrogi, P.4    Szenthe, B.5    Patthy, A.6    Graf, L.7    Katona, G.8
  • 39
    • 0015506470 scopus 로고
    • High Resolution Nuclear Magnetic Resonance Study of the Histidine-Aspartate Hydrogen Bond in Chymotrypsin and Chymotrypsinogen
    • Robillard, G. and Shulman, R. G. (1972) High Resolution Nuclear Magnetic Resonance Study of the Histidine-Aspartate Hydrogen Bond in Chymotrypsin and Chymotrypsinogen J. Mol. Biol. 71, 507-511
    • (1972) J. Mol. Biol. , vol.71 , pp. 507-511
    • Robillard, G.1    Shulman, R.G.2
  • 40
    • 0016148924 scopus 로고
    • High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin
    • Robillard, G. and Shulman, R. G. (1974) High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin J. Mol. Biol. 86, 519-540
    • (1974) J. Mol. Biol. , vol.86 , pp. 519-540
    • Robillard, G.1    Shulman, R.G.2
  • 41
    • 0000072463 scopus 로고
    • Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme
    • Bachovchin, W. W. (1985) Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme Proc. Natl. Acad. Sci. U.S.A. 82, 7948-7951
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 7948-7951
    • Bachovchin, W.W.1
  • 42
    • 0028040716 scopus 로고
    • A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Proteases
    • Frey, P. A., Whitt, S. A., and Tobin, J. B. (1994) A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Proteases Science 264, 1927-1930
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3
  • 43
    • 0032438194 scopus 로고    scopus 로고
    • Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin
    • Lin, J., Westler, W. M., Cleland, W. W., Markley, J. L., and Frey, P. A. (1998) Fractionation factors and activation energies for exchange of the low barrier hydrogen bonding proton in peptidyl trifluoromethyl ketone complexes of chymotrypsin Proc. Natl. Acad. Sci. U.S.A. 95, 14664-14668
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14664-14668
    • Lin, J.1    Westler, W.M.2    Cleland, W.W.3    Markley, J.L.4    Frey, P.A.5
  • 44
    • 0033901427 scopus 로고    scopus 로고
    • The deuterium isotope effect on the NMR signal of the low-barrier hydrogen bond in a transition-state analog complex of chymotrypsin
    • Cassidy, C. S., Lin, J., and Frey, P. A. (2000) The deuterium isotope effect on the NMR signal of the low-barrier hydrogen bond in a transition-state analog complex of chymotrypsin Biochem. Biophys. Res. Commun. 273, 789-792
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 789-792
    • Cassidy, C.S.1    Lin, J.2    Frey, P.A.3
  • 45
    • 0037165710 scopus 로고    scopus 로고
    • Evidence for a strong hydrogen bond in the catalytic dyad of transition-state analogue inhibitor complexes of chymotrypsin from proton-triton NMR isotope shifts
    • Westler, W. M., Frey, P. A., Lin, J., Wemmer, D. E., Morimoto, H., Williams, P. G., and Markley, J. L. (2002) Evidence for a strong hydrogen bond in the catalytic dyad of transition-state analogue inhibitor complexes of chymotrypsin from proton-triton NMR isotope shifts J. Am. Chem. Soc. 124, 4196-4197
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4196-4197
    • Westler, W.M.1    Frey, P.A.2    Lin, J.3    Wemmer, D.E.4    Morimoto, H.5    Williams, P.G.6    Markley, J.L.7
  • 46
    • 0032566351 scopus 로고    scopus 로고
    • Correlations of the basicity of His 57 with transition state analogue binding, substrate reactivity, and the strength of the low-barrier hydrogen bond in chymotrypsin
    • Lin, J., Cassidy, C. S., and Frey, P. A. (1998) Correlations of the basicity of His 57 with transition state analogue binding, substrate reactivity, and the strength of the low-barrier hydrogen bond in chymotrypsin Biochemistry 37, 11940-11948
    • (1998) Biochemistry , vol.37 , pp. 11940-11948
    • Lin, J.1    Cassidy, C.S.2    Frey, P.A.3
  • 47
    • 78751489563 scopus 로고    scopus 로고
    • Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate
    • Zhou, Y. Z. and Zhang, Y. K. (2011) Serine protease acylation proceeds with a subtle re-orientation of the histidine ring at the tetrahedral intermediate Chem. Commun. 47, 1577-1579
    • (2011) Chem. Commun. , vol.47 , pp. 1577-1579
    • Zhou, Y.Z.1    Zhang, Y.K.2
  • 48
    • 0018438406 scopus 로고
    • Do cleavages of amides by serine proteases occur through a stepwise pathway involving tetrahedral intermediates?
    • Komiyama, M. and Bender, M. L. (1979) Do cleavages of amides by serine proteases occur through a stepwise pathway involving tetrahedral intermediates? Proc. Natl. Acad. Sci. U.S.A. 76, 557-560
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 557-560
    • Komiyama, M.1    Bender, M.L.2


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