Chymotrypsin

Handbook of Proteolytic Enzymes

Volumn 3, Issue , 2013, Pages 2626-2633

  Gráf, Lászlo ^a   Szilágyi, Lászlo ^a   Venekei, István ^a  

^a EÖTVÖS LORÁND UNIVERSITY   (Hungary)

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Indexed keywords

EID: 84884669795     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382219-2.00582-2     Document Type: Chapter

References (87)

1. Kühne W. Über die Verdauung der Eiweisstoffe durch den Pankreassaft. Virchows Arch. 1867, 39:130. (reproduced by Gutfreund, H. (1976). FEBS Lett. 62(Suppl.), E1-E12.
2. Northrop J.H., Kunitz M. Crystalline trypsin. I. Isolation and tests of purity. J. Gen. Physiol. 1932, 16(2):267-294.
3. Northrop J.H., Kunitz M., Herriott R.M. Crystalline Enzymes 1939, Columbia University Press, New York.
4. Kunitz M., Northrop J.H. Crystalline chymo-trypsin and chymo-trypsinogen. I. Isolation, crystallization, and general properties of a new proteolytic enzyme and its precursor. J. Gen. Physiol. 1935, 18(4):433-458.
5. Laskowski M. Chymotrypsinogens and chymotrypsins. Methods Enzymol. 1955, 2:8-26.
6. Hartley B.S. Amino-acid sequence of bovine chymotrypsinogen-A. Nature 1964, 201:1284-1287.
7. Meloun B., Kluh I., Kostka V., Morávek L., Pruśik Z., Vaněcek J., Keil B., Šorm F. Covalent structure of bovine chymotrypsinogen A. Biochim. Biophys. Acta 1966, 130:543-546.
8. Smillie L.B., Furka A., Nagabhushan N., Stevenson K.J., Parkes C.O. Structure of chymotrypsinogen B compared with chymotrypsinogen A and trypsinogen. Nature 1968, 218:343-346.
9. Tomita N., Izumoto Y., Horii A., Doi S., Yokouchi H., Ogawa M., Mori T., Matsubara K. Molecular cloning and nucleotide sequence of human pancreatic prechymotrypsinogen cDNA. Biochem. Biophys. Res. Commun. 1989, 158(2):569-575.
10. Bell G.I., Quinto C., Quiroga M., Valenzuela P., Craik C.S., Rutter W.J. Isolation and sequence of a rat chymotrypsin B gene. J. Biol. Chem. 1984, 259:14265-14270.
11. Jacobsen C.F. C R Trav Lab Carlsberg 1947, 25:325-347.
12. Desnuelle, P. (1960). Chymotrypsin. In 118, 1 edn (Boyer, P.D., Lardy, H., Myrback, K. eds), pp. 93-118, Academic Press, New York.
13. Cohen G.H., Silverton E.W., Davies D.R. Refined crystal structure of gamma-chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases. J. Mol. Biol. 1981, 148(4):449-479.
14. Neurath H. The activation of zymogens. Advances in Protein Chemistry 1957, 12:319-386. Academic Press, New York.
15. Huber R., Bode W. Structural basis of the activation and action of trypsin. Acc. Chem. Res. 1978, 11:114-122.
16. Bergmann M., Fruton J.S. The specificity of proteinases. Adv. Enzymol. 1941, 1:63-98.
17. Gráf L. Structural basis of serine protease action: the fourth dimension. Natural Sciences and Human Thought 1995, 139-148. Springer-Verlag, Berlin, Heidelberg. R. Zwilling (Ed.).
18. Perona J.J., Craik C.S. Structural basis of substrate specificity in the serine proteases. Protein Sci. 1995, 4(3):337-360.
19. Venekei I., Gráf L., Rutter W.J. Expression of rat chymotrypsinogen in yeast: a study on the structural and functional significance of the chymotrypsinogen propeptide. FEBS Lett. 1996, 379:139-142.
20. Keller P.J., Cohen E., Neurath H. The proteins of bovine pancreatic juice. J. Biol. Chem. 1958, 233:344-349.
21. Bender M.L. The mechanism of alpha-chymotrypsin-catalyzed hydrolyses. J. Am. Chem. Soc. 1962, 84(13):2582-2590.
22. Hartley B.S., Kilby B.A. The reaction of p-nitrophenyl esters with chymotrypsin and insulin. Biochem. J. 1954, 56:288-297.
23. Henderson R. Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme. J. Mol. Biol. 1970, 54(2):341-354.
24. Henderson R., Wright C.S., Hess G.P., Blow D.M. alpha-Chymotrypsin: what can we learn about catalysis from x-ray diffraction?. Cold Spring Harb. Symp. Quant. Biol. 1972, 36:63-70.
25. Stoddard B.L., Bruhnke J., Porter N., Ringe D., Petsko G.A. Structure and activity of two photoreversible cinnamates bound to chymotrypsin. Biochemistry 1990, 29(20):4871-4879.
26. Stoddard B.L., Bruhnke J., Koenigs P., Porter N., Ringe D., Petsko G.A. Photolysis and decaylation of inhibited chymotrypsin. Biochemistry 1990, 29(35):8042-8051.
27. Fastrez J., Fersht A.R. Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin. Biochemistry 1973, 12:2025-2034.
28. Dixon M.M., Matthews B.W. Is gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin?. Biochemistry 1989, 28(17):7033-7038.
29. Dixon M.M., Brennan R.G., Matthews B.W. Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH. Int. J. Biol. Macromol. 1991, 13(2):89-96.
30. Harel M., Su C.T., Frolow F., Silman I., Sussman J.L. Gamma-chymotrypsin is a complex of alpha-chymotrypsin with its own autolysis products. Biochemistry 1991, 30(21):5217-5225.
31. Yennawar N.H., Yennawar H.P., Farber G.K. X-ray crystal structure of gamma-chymotrypsin in hexane. Biochemistry 1994, 33(23):7326-7336.
32. Jameson G.W., Roberts D.V., Adams R.W., Kyle W.S., Elmore D.T. Determination of the operational molarity of solutions of bovine alpha-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorimetric titration. Biochem. J. 1973, 131:107-117.
33. 2-macroglobulin and high-performance liquid chromatography. Anal. Biochem. 1992, 207:76-79.
34. Hill R.L. Hydrolysis of proteins. Advances in Protein Chemistry 1965, vol. 20:68-74. Academic Press, New York.
35. Schellenberger V., Braune K., Hofmann H.J., Jakubke H.D. The specificity of chymotrypsin. A statistical analysis of hydrolysis data. Eur. J. Biochem. 1991, 199:623-636.
36. Duan Y., Laursen R.A. Protease substrate specificity mapping using membrane-bound peptides. Anal. Biochem. 1994, 216(2):431-438.
37. Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 1967, 27:157-162.
38. DelMar E.G., Largman C., Brodrick J.W., Geokas M.C. A sensitive new substrate for chymotrypsin. Anal. Biochem. 1979, 99:316-320.
39. Harper J.W., Ramirez G., Powers J.C. Reaction of peptide thiobenzyl esters with mammalian chymotrypsin-like enzymes: a sensitive assay method. Anal. Biochem. 1981, 118:382-387.
40. Monsees T., Miska W., Geiger R. Synthesis and characterization of a bioluminogenic substrate for alpha-chymotrypsin. Anal. Biochem. 1994, 221:329-334.
41. Fisher G., Bang H., Berger E., Schellenberger A. Conformational specificity of chymotrypsin toward proline containing substrates. Biochem. Biophys. Acta 1984, 791:87-97.
42. Lang K., Schmid F.X. Protein-disulphide isomerase and prolyl isomerase act differently and independently as catalysts of protein folding. Nature 1988, 331(6155):453-455.
43. Jansen E.F., Nutting F., Balls A.K. Mode of inhibition of chymotrypsin by diisopropylfluorophosphate; introduction of phosphorus. J. Biol. Chem. 1949, 179(1):201-204.
44. Lively M.O., Powers J.C. Specificity and reactivity of human granulocyte elastase and cathepsin G, porcine pancreatic elastase, bovine chymotrypsin and trypsin toward inhibition with sulfonyl fluorides. Biochim. Biophys. Acta 1978, 525:171-179.
45. Harper J.W., Hemmi K., Powers J.C. Reaction of serine proteases with substituted isocoumarins: discovery of 3,4-dichloroisocoumarin, a new general mechanism based serine protease inhibitor. Biochemistry 1985, 24:1831-1841.
46. Umezawa, H., Aoyagi, T. (1977). Activities of proteinase inhibitors of microbial origin, in 662, Barrett, A.J., ed. North-Holland Publishing Company, Amsterdam, pp. 637-662.
47. Fujinaga M., Sielecki A.R., Read R.J., Ardelt W., Laskowski M., James M.N. Crystal and molecular structures of the complex of alpha-chymotrypsin with its inhibitor turkey ovomucoid third domain at 1.8Å resolution. J. Mol. Biol. 1987, 195(2):397-418.
48. Delaria K.A., Muller D.K., Marlor C.W., Brown J.E., Das R.C., Roczniak S.O., Tamburini P.P. Characterization of placental bikunin, a novel human serine protease inhibitor. J. Biol. Chem. 1997, 272(18):12209-12214.
49. Takano R., Imada C., Kamei K., Hara S. The reactive site of marinostatin, a proteinase inhibitor from marine Alteromonas sp. B-10-31. J. Biochem. 1991, 110(6):856-858.
50. Baici A., Seemuller U. Kinetics of the inhibition of human leucocyte elastase by eglin from the leech Hirudo medicinalis. Biochem. J. 1984, 218(3):829-833.
51. Spink E., Cosgrove S., Rogers L., Hewage C., Malthouse J.P. 13C and 1H NMR studies of ionizations and hydrogen bonding in chymotrypsin-glyoxal inhibitor complexes. J. Biol. Chem. 2007, 282(11):7852-7861.
52. Spink E., Hewage C., Malthouse J.P. Determination of the structure of tetrahedral transition state analogues bound at the active site of chymotrypsin using 18O and 2H isotope shifts in the 13C NMR spectra of glyoxal inhibitors. Biochemistry 2007, 46(44):12868-12874.
53. Singh N., Jabeen T., Sharma S., Roy I., Gupta M.N., Bilgrami S., Somvanshi R.K., Dey S., Perbandt M., Betzel C., Srinivasan A., Singh T.P. Detection of native peptides as potent inhibitors of enzymes. Crystal structure of the complex formed between treated bovine alpha-chymotrypsin and an autocatalytically produced fragment, IIe-Val-Asn-Gly-Glu-Glu-Ala-Val-Pro-Gly-Ser-Trp-Pro-Trp, at 2.2 angstroms resolution. FEBS J. 2005, 272(2):562-572.
54. Marquart M., Walter J., Deisenhofer J., Bode W., Huber R. Acta Crystallogr 1983, B39:480-490.
55. Ohara T., Makino K., Shinagawa H., Nakata A., Norioka S., Sakiyama F. Cloning, nucleotide sequence, and expression of Achromobacter protease I gene. J. Biol. Chem. 1989, 264(34):20625-20631.
56. Bazan J.F., Fletterick R.J. Structural and catalytic models of trypsin-like viral proteases. Semin. Virol. 1990, 1:311-322.
57. McGrath M.E., Vásquez J.R., Craik C.S., Yang A.S., Honig B., Fletterick R.J. Perturbing the polar environment of Asp102 in trypsin: consequences of replacing conserved Ser214. Biochemistry 1992, 31(12):3059-3064.
58. Blow D.M. Structure and mechanism of chymotrypsin. Acc. Chem. Res. 1976, 9(4):145-152.
59. Ruhlmann A., Kukla D., Schwager P., Bartels K., Huber R. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region. J. Mol. Biol. 1973, 77:417-436.
60. Steitz T.A., Henderson R., Blow D.M. Structure of crystalline alpha-chymotrypsin. 3. Crystallographic studies of substrates and inhibitors bound to the active site of alpha-chymotrypsin. J. Mol. Biol. 1969, 46:337-348.
61. Brady K., Wei A.Z., Ringe D., Abeles R.H. Structure of chymotrypsin-trifluoromethyl ketone inhibitor complexes: comparison of slowly and rapidly equilibrating inhibitors. Biochemistry 1990, 29(33):7600-7607.
62. Hudaky P., Perczel A. A self-stabilized model of the chymotrypsin catalytic pocket. The energy profile of the overall catalytic cycle. Proteins 2006, 62:749-759.
63. Dorovskaya V.N., Varfolomeyev S.D., Kazanskaya N.F., Klyosov A.A., Martinek K. The influence of the geometric properties of the active centre on the specificity of α-chymotrypsin catalysis. FEBS Lett. 1972, 23:122.
64. Gráf L., Jancsó A., Szilágyi L., Hegyi G., Pintér K., Náray-Szabó G., Hepp J., Medzihradszky K., Rutter W.J. Electrostatic complementarity within the substrate-binding pocket of trypsin. Proc. Natl. Acad. Sci. USA 1988, 85:4961-4965.
65. Perona J.J., Hedstrom L., Wagner R.L., Rutter W.J., Craik C.S., Fletterick R.J. Exogenous acetate reconstitutes the enzymatic activity of trypsin Asp189Ser. Biochemistry 1994, 33:3252-3259.
66. Venekei I., Szilágyi L., Gráf L., Rutter W.J. Attempts to convert chymotrypsin to trypsin. FEBS Lett. 1996, 383(1-2):143-147.
67. Szabó E., Venekei I., Bocskei Z., Náray-Szabó G., Gráf L. Three dimensional structures of S189D chymotrypsin and D189S trypsin mutants: the effect of polarity at site 189 on a protease-specific stabilization of the substrate-binding site. J. Mol. Biol. 2003, 331(5):1121-1130.
68. Jelinek B., Antal J., Venekei I., Gráf L. Ala226 to Gly and Ser189 to Asp mutations convert rat chymotrypsin B to a trypsin-like protease. Protein Eng. Des. Sel. 2004, 17(2):127-131.
69. Jelinek B., Katona G., Fodor K., Venekei I., Gráf L. The crystal structure of a trypsin-like mutant chymotrypsin: the role of position 226 in the activity and specificity of S189D chymotrypsin. Protein J. 2008, 27(2):79-87.
70. Hedstrom L., Szilágyi L., Rutter W.J. Converting trypsin to chymotrypsin: the role of surface loops. Science 1992, 255(5049):1249-1253.
71. Hedstrom L., Perona J.J., Rutter W.J. Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant. Biochemistry 1994, 33(29):8757-8763.
72. Hedstrom L., Farr-Jones S., Kettner C.A., Rutter W.J. Converting trypsin to chymotrypsin: ground-state binding does not determine substrate specificity. Biochemistry 1994, 33(29):8764-8769.
73. Perona J.J., Hedstrom L., Rutter W.J., Fletterick R.J. Structural origins of substrate discrimination in trypsin and chymotrypsin. Biochemistry 1995, 34:1489-1499.
74. Markley J.L. Catalytic groups of serine proteinases. NMR investigations. Magnetic Resonance Studies in Biology 1979, 397-461. Academic Press, New York. R.G. Shulman (Ed.).
75. Sigler P.B., Blow D.M., Matthews B.W., Henderson R. Structure of crystalline alpha-chymotrypsin. II. A preliminary report including a hypothesis for the activation mechanism. J. Mol. Biol. 1968, 35:143-164.
76. Wang D., Bode W., Huber R. Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8Å resolution. J. Mol. Biol. 1985, 185(3):595-624.
77. Varallyay E., Lengyel Z., Gráf L., Szilágyi L. The role of disulfide bond C191-C220 in trypsin and chymotrypsin. Biochem. Biophys. Res. Commun. 1997, 230:592-596.
78. Wilcox P.E. Chymotrypsinogens - chymotrypsins. Methods Enzymol. 1970, 19:64-108.
79. Schellenberger V., Turck C.W., Hedstrom L., Rutter W.J. Mapping the S' subsites of serine proteases using acyl transfer to mixtures of peptide nucleophiles. Biochemistry 1993, 32(16):4349-4353.
80. Kaslik G., Patthy A., Bálint M., Gráf L. Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibility. FEBS Lett. 1995, 370(3):179-183.
81. Kaslik G., Kardos J., Szabó E., Szilágyi L., Závodszky P., Westler W.M., Markley J.L., Gráf L. Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active site. Biochemistry 1997, 36:5455-5464.
82. Plotnick M.I., Mayne L., Schechter N.M., Rubin H. Distortion of the active site of chymotrypsin complexed with a serpin. Biochemistry 1996, 35(23):7586-7590.
83. Miao Q., Sun Y., Wei T., Zhao X., Zhao K., Yan L., Zhang X., Shu H., Yang F. Chymotrypsin B cached in rat liver lysosomes and involved in apoptotic regulation through a mitochondrial pathway. J. Biol. Chem. 2008, 283(13):8218-8228.
84. Zhao K., Zhao X., Tu Y., Miao Q., Cao D., Duan W., Sun Y., Wang J., Wei T., Yang F. Lysosomal chymotrypsin B potentiates apoptosis via cleavage of Bid. Cell Mol. Life Sci. 2010, 67(15):2665-2678.
85. Abita J.P., Delaage M., Lazdunski M. The mechanism of activation of trypsinogen. The role of the four N-terminal aspartyl residues. Eur. J. Biochem. 1969, 8:314-324.
86. Timasheff S.N. On the mechanism of alpha-chymotrypsin dimerization. Arch. Biochem. Biophys. 1969, 132(1):165-169.
87. Aune K.C., Timasheff S.N. Dimerization of alpha-chymotrypsin. I. pH dependence in the acid region. Biochemistry 1971, 10(9):1609-1617.