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PMID: 6758764 Published · ppublish English Journal Article Review

Current problems in mechanistic studies of serine and cysteine proteinases.

The Biochemical journal ·Vol. 207 ·No. 1 ·1982-10-01 ·Pages 1-10

Polgár L, Halász P

Abstract

暂无摘要

MeSH Terms
Aspartic Acid/metabolism Binding Sites Catalysis Cysteine/metabolism Cysteine Endopeptidases Endopeptidases/metabolism Histidine/metabolism Models, Chemical Papain/metabolism Protein Conformation Serine Endopeptidases
Chemicals
Aspartic Acid Histidine Endopeptidases Serine Endopeptidases Cysteine Endopeptidases Papain Cysteine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Polgár L
Halász P
References (92)
92 references, click to expand
  1. Structure of crystalline -chymotrypsin. V. The atomic structure of tosyl- -chymotrypsin at 2 A resolution.
    J Mol Biol. 1972 Jul 21;68(2):187-240 PMID: 5069789
  2. Neutron diffraction identifies His 57 as the catalytic base in trypsin.
    Nature. 1980 Nov 27;288(5789):414-6 PMID: 7432541
  3. Deuterium isotope effects on papain acylation. Evidence for lack of general base catalysis and for enzyme--leaving-group interaction.
    Eur J Biochem. 1979 Aug 1;98(2):369-74 PMID: 488108
  4. Lack of evidence for a tetrahedral intermediate in the hydrolysis of nitroanilide substrates by serine proteinases. Subzero-temperature stopped-flow experiments.
    Eur J Biochem. 1981 Dec;120(3):477-85 PMID: 6460615
  5. Differences in the interaction of the catalytic groups of the active centres of actinidin and papain. Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes.
    Biochem J. 1981 Sep 1;197(3):739-46 PMID: 7034724
  6. Refined crystal structure of gamma-chymotrypsin at 1.9 A resolution. Comparison with other pancreatic serine proteases.
    J Mol Biol. 1981 Jun 5;148(4):449-79 PMID: 6914398
  7. Evidence for a close similarity in the catalytic sites of papain and ficin in near-neutral media despite differences in acidic and alkaline media. Kinetics of the reactions of papain and ficin with chloroacetate.
    Biochem J. 1982 Jan 1;201(1):101-4 PMID: 7044370
  8. Evidence for two acyl group conformations in some furylacryloyl- and thienylacryloylchymotrypsins: resonance Raman studies of enzyme--substrate intermediates at pH 3.0.
    Biochemistry. 1981 Jun 9;20(12):3438-47 PMID: 7260048
  9. Evidence that binding to the s2-subsite of papain may be coupled with catalytically relevant structural change involving the cysteine-25-histidine-159 diad. Kinetics of the reaction of papain with a two-protonic-state reactivity probe containing a hydrophobic side chain.
    Biochem J. 1979 Nov 1;183(2):223-31 PMID: 43129
  10. Isolation of highly active papaya peptidases A and B from commercial chymopapain.
    Biochim Biophys Acta. 1981 Apr 14;658(2):262-9 PMID: 7018581
  11. Carbon-13 nuclear magnetic resonance studies of proteins.
    Annu Rev Biophys Bioeng. 1977;6:383-417 PMID: 17352
  12. Crystallographic and kinetic investigations of the covalent complex formed by a specific tetrapeptide aldehyde and the serine protease from Streptomyces griseus.
    Proc Natl Acad Sci U S A. 1979 Jan;76(1):96-100 PMID: 106392
  13. Synthesis and evaluation of a model for the so-called "charge-relay" system of the serine esterases.
    J Am Chem Soc. 1974 Apr 17;96(8):2473-81 PMID: 4833707
  14. Carbon-13 nuclear magnetic resonance studies of the selectively isotope-labeled reactive site peptide bond of the basic pancreatic trypsin inhibitor in the complexes with trypsin, trypsinogen, and anhydrotrypsin.
    Biochemistry. 1980 Dec 9;19(25):5711-5 PMID: 6161642
  15. Zymogen activation in serine proteinases. Proton magnetic resonance pH titration studies of the two histidines of bovine chymotrypsinogen A and chymotrypsin Aalpha.
    Biochemistry. 1978 Oct 31;17(22):4627-40 PMID: 31898
  16. The conversion of serine at the active site of subtilisin to cysteine: a "chemical mutation".
    Proc Natl Acad Sci U S A. 1966 Nov;56(5):1606-11 PMID: 5230319
  17. Crystal structure of elastase-substrate complex at -- 55 degrees C.
    Nature. 1976 Sep 23;263(5575):297-300 PMID: 958484
  18. X-ray crystallographic study of boronic acid adducts with subtilisin BPN' (Novo). A model for the catalytic transition state.
    J Biol Chem. 1975 Sep 25;250(18):7120-6 PMID: 1165237
  19. Benzoylamidoacetonitrile as an inhibitor of papain.
    Biochim Biophys Acta. 1973 Mar 15;302(1):95-101 PMID: 4692655
  20. Mechanism of Action of papain with a specific anilide substrate.
    Biochemistry. 1979 May 29;18(11):2355-63 PMID: 444461
  21. Characterization of the papain active centre by using two-protonic-state electrophiles as reactivity probes. Evidence for nucleophilic reactivity in the un-interrupted cysteine-25-histidine-159 interactive system.
    Biochem J. 1978 May 1;171(2):385-401 PMID: 26335
  22. Mechanism of hydrolysis by serine proteases: direct determination of the pKa's of aspartyl-102 and aspartyl-194 in bovine trypsin using difference infrared spectroscopy.
    Biochemistry. 1976 Aug 10;15(16):3450-8 PMID: 986162
  23. Detection of a tetrahedral intermediate in the trypsin-catalysed hydrolysis of specific ring-activated anilides.
    Biochim Biophys Acta. 1978 Apr 12;523(2):538-41 PMID: 566121
  24. The nature of general base-general acid catalysis in serine proteases.
    Proc Natl Acad Sci U S A. 1969 Dec;64(4):1335-42 PMID: 5271756
  25. Negatively charged reactants as probes in the study of the essential mercaptide-imidazolium ion-pair of thiolenzymes.
    Eur J Biochem. 1977 Oct 3;79(2):491-4 PMID: 923564
  26. On the stereochemistry of catalysis by serine proteases.
    J Theor Biol. 1974 Aug;46(2):543-58 PMID: 4420762
  27. Role of a buried acid group in the mechanism of action of chymotrypsin.
    Nature. 1969 Jan 25;221(5178):337-40 PMID: 5764436
  28. Dependence of the catalytic activity of papain on the ionization of two acidic groups.
    J Biol Chem. 1978 Jul 25;253(14):5080-6 PMID: 27512
  29. Mechanism of association of N-acetyl-L-phenylalanylglycinal to papain.
    Biochemistry. 1981 Sep 15;20(19):5517-24 PMID: 7295689
  30. ACTIVATION OF STREPTOCOCCAL PROTEINASE AND ITS ZYMOGEN BY BACTERIAL CELL WALLS.
    Nature. 1965 Apr 3;206:33-4 PMID: 14334353
  31. Nitrogen isotope effects on the chymotrypsin-catalyzed hydrolysis of N-acetyl-L-tryptophanamide.
    J Am Chem Soc. 1972 May 17;94(10):3585-9 PMID: 5032959
  32. Energetics of enzyme catalysis.
    Proc Natl Acad Sci U S A. 1978 Nov;75(11):5250-4 PMID: 281676
  33. Evidence for multiple reactive forms of papain.
    Eur J Biochem. 1978 Aug 1;88(2):513-21 PMID: 689035
  34. Evidence for a two-state transition in papain that may have no close analogue in ficin. Differences in the disposition of cationic sites and hydrophobic binding areas in the active centres of papain and ficin.
    Biochem J. 1980 Dec 1;191(3):707-18 PMID: 7025834
  35. Structure of actinidin, after refinement at 1.7 A resolution.
    J Mol Biol. 1980 Aug 25;141(4):441-84 PMID: 7003158
  36. Mechanism-controlled stereospecificity. Acylation of subtilisin with enantiomeric alkyl and nitrophenyl ester substrates.
    Eur J Biochem. 1979 Dec 17;102(2):531-6 PMID: 43249
  37. IV. Cysteine proteinases. The structure of the papain molecule.
    Philos Trans R Soc Lond B Biol Sci. 1970 Feb 12;257(813):231-6 PMID: 4399047
  38. Effect of cysteine-25 on the ionization of histidine-159 in papain as determined by proton nuclear magnetic resonance spectroscopy. Evidence for a his-159--Cys-25 ion pair and its possible role in catalysis.
    Biochemistry. 1981 Jan 6;20(1):48-51 PMID: 7470479
  39. Re-examination of the charge relay system in subtilisin comparison with other serine proteases.
    J Biol Chem. 1977 Dec 25;252(24):8875-83 PMID: 21885
  40. A kinetic and fluorimetric investigation of papain modified at tryptophan-69 and -177 by N-bromosuccinimide.
    Biochem J. 1974 Aug;141(2):503-15 PMID: 4455219
  41. Proton nuclear magnetic resonance evidence for the absence of a stable hydrogen bond between the active site aspartate and histidine residues of native subtilisins and for its presence in thiolsubtilisins.
    Biochemistry. 1981 Oct 27;20(22):6366-70 PMID: 7030388
  42. DIRECT EVIDENCE FOR AN ACYLATED THIOL AS AN INTERMEDIATE IN PAPAIN- AND FICIN-CATALYSED HYDROLYSES.
    Biochem J. 1965 Jul;96:189-93 PMID: 14343129
  43. On the role of hydrogen-bonding system in the catalysis by serine proteases.
    Acta Biochim Biophys Acad Sci Hung. 1972;7(1):29-34 PMID: 5084288
  44. Evidence for histidine in the active site of papain.
    Biochem J. 1968 Aug;108(5):855-9 PMID: 5673530
  45. The fluorescence of papain.
    Biochim Biophys Acta. 1970 Mar 31;200(3):595-7 PMID: 5436651
  46. Mechanism of thiol protease catalysis: detection and stabilization of a tetrahedral intermediate in papain catalysis.
    Biochemistry. 1979 May 29;18(11):2363-9 PMID: 36130
  47. Perturbations in the free energy and enthalpy of ionization of histidine-159 at the active site of papain as determined by fluorescence spectroscopy.
    Biochemistry. 1981 Jan 6;20(1):52-8 PMID: 7470480
  48. A spectroscopic investigation of S-trifluoroethylthiopapain. An investigation of the active site of papain.
    Eur J Biochem. 1976 Jun 1;65(2):493-502 PMID: 7453
  49. Cryoenzymology of papain: reaction mechanism with an ester substrate.
    Biochemistry. 1978 Jun 27;17(13):2659-68 PMID: 678536
  50. Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer.
    Biochemistry. 1976 Dec 14;15(25):5581-8 PMID: 999831
  51. The importance of the conformation of the tetrahedral intermediate for the alpha-chymotrypsin-catalyzed hydrolysis of peptide substrates.
    FEBS Lett. 1975 Nov 1;59(1):105-8 PMID: 1225610
  52. Analogy between active sites of cathepsin B(1) and papain.
    FEBS Lett. 1970 Dec 11;11(4):287-288 PMID: 11945508
  53. A purification and some properties of two proteases from papaya latex.
    Biochim Biophys Acta. 1979 Aug 15;569(2):193-201 PMID: 476125
  54. Structure of crystalline alpha-chymotrypsin. IV. The structure of indoleacryloyl-alpha-chyotrypsin and its relevance to the hydrolytic mechanism of the enzyme.
    J Mol Biol. 1970 Dec 14;54(2):341-54 PMID: 5494034
  55. Crystal structure of the complex of porcine trypsin with soybean trypsin inhibitor (Kunitz) at 2.6-A resolution.
    Biochemistry. 1974 Sep 24;13(20):4212-28 PMID: 4472048
  56. Potentiometric determination of ionizations at the active site of papain.
    Biochemistry. 1976 Nov 16;15(23):5009-17 PMID: 10964
  57. Purification and characterization of vicilin peptidohydrolase, the major endopeptidase in the cotyledons of mung-bean seedlings.
    Eur J Biochem. 1977 Jul 15;77(2):223-33 PMID: 891531
  58. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution.
    J Mol Biol. 1974 Oct 15;89(1):73-101 PMID: 4475115
  59. Soybean trypsin inhibitor (Kunitz) and its complex with trypsin. Carbon-13 nuclear magnetic resonance studies of the reactive site arginine.
    Biochemistry. 1980 Dec 9;19(25):5703 PMID: 7459339
  60. MECHANISM OF ACTION OF PROTEOLYTIC ENZYMES.
    Annu Rev Biochem. 1965;34:49-76 PMID: 14321178
  61. Subtilisin; a stereochemical mechanism involving transition-state stabilization.
    Biochemistry. 1972 Nov 7;11(23):4293-303 PMID: 5079900
  62. The preparation and properties of trans-cinnamoyl-papain.
    J Am Chem Soc. 1966 Dec 20;88(24):5871-80 PMID: 5980875
  63. The detection, accumulation and stabilization of a tetrahedral intermediate in trypsin catalysis.
    Biochem Biophys Res Commun. 1980 Mar 28;93(2):427-31 PMID: 6770851
  64. One-proton catalysis in the deacetylation of acetyl- -chymotrypsin.
    J Am Chem Soc. 1973 Feb 7;95(3):968-9 PMID: 4688663
  65. Do cleavages of amides by serine proteases occur through a stepwise pathway involving tetrahedral intermediates?
    Proc Natl Acad Sci U S A. 1979 Feb;76(2):557-60 PMID: 284381
  66. Catalysis and leaving group binding in anilide hydrolysis by chymotrypsin.
    Biochim Biophys Acta. 1978 Nov 10;527(1):131-41 PMID: 718954
  67. Stoichiometry of the nitrous acid deaminative cleavage of model amino sugar glycosides and glycosaminoglycuronans.
    Biochemistry. 1970 Jan 6;9(1):33-43 PMID: 4243761
  68. Three-dimensional structure of tosyl-alpha-chymotrypsin.
    Nature. 1967 May 13;214(5089):652-6 PMID: 6049071
  69. Is the thiolate--imidazolium ion pair the catalytically important form of papain?
    FEBS Lett. 1980 Feb 11;110(2):319-22 PMID: 7371836
  70. Multiple forms of the asclepains. Cysteinyl proteases from milkweed.
    Biochim Biophys Acta. 1980 Mar 14;612(1):119-25 PMID: 6988008
  71. Solvent isotope effects on tautomerization equilibria of papain and model thiolamines.
    FEBS Lett. 1980 Feb 11;110(2):313-8 PMID: 7371835
  72. Kinetic specificity in papain-catalysed hydrolyses.
    Biochem J. 1971 Aug;124(1):107-15 PMID: 5126466
  73. High resolution nuclear magnetic resonance study of the histidine--aspartate hydrogen bond in chymotrypsin and chymotrypsinogen.
    J Mol Biol. 1972 Nov 14;71(2):507-11 PMID: 4635995
  74. Binding of chloromethyl ketone substrate analogues to crystalline papain.
    Biochemistry. 1976 AUG 24;15(17):3731-8 PMID: 952885
  75. Protein structure refinement: Streptomyces griseus serine protease A at 1.8 A resolution.
    J Mol Biol. 1979 Nov 15;134(4):781-804 PMID: 119870
  76. Serine proteases: structure and mechanism of catalysis.
    Annu Rev Biochem. 1977;46:331-58 PMID: 332063
  77. Purification and preliminary characterization of two asclepains from the latex of Asclepias syriaca L. (milkweed).
    Biochim Biophys Acta. 1979 May 23;578(1):13-22 PMID: 36921
  78. Detection and accumulation of tetrahedral intermediates in elastase catalysis.
    Proc Natl Acad Sci U S A. 1979 Apr;76(4):1566-9 PMID: 36609
  79. Structure of actinidin: details of the polypeptide chain conformation and active site from an electron density map at 2-8 A resolution.
    J Mol Biol. 1977 Sep 25;115(3):263-77 PMID: 592367
  80. Carbon nuclear magnetic resonance studies of the histidine residue in alpha-lytic protease. Implications for the catalytic mechanism of serine proteases.
    Biochemistry. 1973 Nov 6;12(23):4732-43 PMID: 4204227
  81. The refined crystal structure of bovine beta-trypsin at 1.8 A resolution. II. Crystallographic refinement, calcium binding site, benzamidine binding site and active site at pH 7.0.
    J Mol Biol. 1975 Nov 15;98(4):693-717 PMID: 512
  82. Mercaptide-imidazolium ion-pair: the reactive nucleophile in papain catalysis.
    FEBS Lett. 1974 Oct 1;47(1):15-8 PMID: 4426388
  83. Structure of papain.
    Nature. 1968 Jun 8;218(5145):929-32 PMID: 5681232
  84. The structure of papain.
    Adv Protein Chem. 1971;25:79-115 PMID: 4946704
  85. Role of Asp102 in the enzymatic reaction of bovine beta-trypsin. A molecular orbital study.
    J Mol Biol. 1981 Aug 15;150(3):409-21 PMID: 6795358
  86. Dimerization of papain induced by mercuric chloride and a bifunctional organic mercurial.
    Eur J Biochem. 1977 Jul 1;77(1):107-11 PMID: 198207
  87. Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: neutron structure of trypsin.
    Biochemistry. 1981 Oct 27;20(22):6462-74 PMID: 7030393
  88. 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 Jul 5;77(3):417-36 PMID: 4737866
  89. Chemical modification of one carboxyl-group of papain abolishes the catalytic activity of the enzyme.
    FEBS Lett. 1974 Sep 1;45(1):79-81 PMID: 4412409
  90. Co-operative ionisation of aspartic-acid-158 and histidine-159 in papain. Evidence from 19F nuclear-magnetic-resonance and fluorescence spectroscopy.
    Eur J Biochem. 1976 Jun 1;65(2):481-91 PMID: 949979
  91. Effects of substituents on the rates of deacylation of substituted benzoyl papains. Role of a carboxylate residue in the catalytic mechanism.
    Biochemistry. 1978 Jun 27;17(13):2669-74 PMID: 28148
  92. Proton equilibria in the binding of Zn2+ and of methylmercuric iodide to papain.
    Eur J Biochem. 1976 Dec 11;71(2):383-91 PMID: 12964
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2070001
Published
1982-10-01
Pages
1-10
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1153816
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2070001 PMC Full Text View journal details
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