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1
A marked gradation in active-centre properties in the cysteine proteinases revealed by neutral and anionic reactivity probes. Reactivity characteristics of the thiol groups of actinidin, ficin, papain and papaya peptidase A towards 4,4'-dipyridyl disulphide and 5,5'-dithiobis-(2-nitrobenzoate) dianion.
Biochem J. 1983 Mar 1;209(3):873-9. doi: 10.1042/bj2090873.
2
Characterization of papaya peptidase A as a cysteine proteinase of Carica papaya L. with active-centre properties that differ from those of papain by using 2,2'-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as reactivity probes. Use of two-protonic-state electrophiles in the identification of catalytic-site thiol groups.
Biochem J. 1982 Jul 1;205(1):205-11. doi: 10.1042/bj2050205.
3
Evidence that the active centre of chymopapain A is different from the active centres of some other cysteine proteinases and that the Brønsted coefficient (beta nuc.) for the reactions of thiolate anions with 2,2'-dipyridyl disulphide may be decreased by reagent protonation.
Biochem J. 1980 Jul 1;189(1):189-29. doi: 10.1042/bj1890189.
4
Reactivities of neutral and cationic forms of 2,2'-dipyridyl disulphide towards thiolate anions. Detection of differences between the active centres of actinidin, papain and ficin by a three-protonic-state reactivity probe.
Biochem J. 1979 Nov 1;183(2):233-8. doi: 10.1042/bj1830233.
5
Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives.
Biochem J. 1986 Jan 1;233(1):119-29. doi: 10.1042/bj2330119.
6
Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase omega. Three-dimensional structure of papaya proteinase omega deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis.
Biochem J. 1991 Nov 15;280 ( Pt 1)(Pt 1):79-92. doi: 10.1042/bj2800079.
7
Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain.
Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):805-20. doi: 10.1042/bj3000805.
8
A kinetic method for the study of solvent environments of thiol groups in proteins involving the use of a pair of isomeric reactivity probes and a differential solvent effect. Investigation of the active centre of ficin by using 2,2'- and 4,4'- dipyridyl disulphides as reactivity probes.
Biochem J. 1980 Jan 1;185(1):217-22. doi: 10.1042/bj1850217.
9
Reactions of papain and of low-molecular-weight thiols with some aromatic disulphides. 2,2'-Dipyridyl disulphide as a convenient active-site titrant for papain even in the presence of other thiols.
Biochem J. 1973 May;133(1):67-80. doi: 10.1042/bj1330067.
10
Preparation of fully active ficin from Ficus glabrata by covalent chromatography and characterization of its active centre by using 2,2'-depyridyl disulphide as a reactivity probe.
Biochem J. 1976 Nov;159(2):221-34. doi: 10.1042/bj1590221.
引用本文的文献
1
Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations.
Biochem J. 2001 Jul 15;357(Pt 2):343-52. doi: 10.1042/0264-6021:3570343.
2
Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide).
Biochem J. 1984 Sep 15;222(3):805-14. doi: 10.1042/bj2220805.
3
Differences between the electric fields of the catalytic sites of papain and actinidin detected by using the thiol-located nitrobenzofurazan label as a spectroscopic reporter group.
Biochem J. 1984 Jun 1;220(2):609-12. doi: 10.1042/bj2200609.
4
Subsite differences between the active centres of papaya peptidase A and papain as revealed by affinity chromatography. Purification of papaya peptidase A by ionic-strength-dependent affinity adsorption on an immobilized peptide inhibitor of papain.
Biochem J. 1984 May 1;219(3):727-33. doi: 10.1042/bj2190727.
5
Investigation of the catalytic site of actinidin by using benzofuroxan as a reactivity probe with selectivity for the thiolate-imidazolium ion-pair systems of cysteine proteinases. Evidence that the reaction of the ion-pair of actinidin (pKI 3.0, pKII 9.6) is modulated by the state of ionization of a group associated with a molecular pKa of 5.5.
Biochem J. 1983 Sep 1;213(3):713-8. doi: 10.1042/bj2130713.
6
Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4.
Biochem J. 1985 Apr 15;227(2):511-9. doi: 10.1042/bj2270511.
7
A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H.
Biochem J. 1985 Apr 15;227(2):521-8. doi: 10.1042/bj2270521.
8
Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives.
Biochem J. 1986 Jan 1;233(1):119-29. doi: 10.1042/bj2330119.
9
The electrostatic fields in the active-site clefts of actinidin and papain.
Biochem J. 1988 Aug 15;254(1):235-8. doi: 10.1042/bj2540235.
10
Differences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment.
Biochem J. 1987 Oct 1;247(1):181-93. doi: 10.1042/bj2470181.
本文引用的文献
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A colorimetric method for determining low concentrations of mercaptans.
Arch Biochem Biophys. 1958 Apr;74(2):443-50. doi: 10.1016/0003-9861(58)90014-6.
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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. doi: 10.1042/bj2010101.
3
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. doi: 10.1042/bj1970739.
4
Structure of actinidin, after refinement at 1.7 A resolution.
J Mol Biol. 1980 Aug 25;141(4):441-84. doi: 10.1016/0022-2836(80)90255-7.
5
A kinetic method for the study of solvent environments of thiol groups in proteins involving the use of a pair of isomeric reactivity probes and a differential solvent effect. Investigation of the active centre of ficin by using 2,2'- and 4,4'- dipyridyl disulphides as reactivity probes.
Biochem J. 1980 Jan 1;185(1):217-22. doi: 10.1042/bj1850217.
6
Characterization of papaya peptidase A as a cysteine proteinase of Carica papaya L. with active-centre properties that differ from those of papain by using 2,2'-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as reactivity probes. Use of two-protonic-state electrophiles in the identification of catalytic-site thiol groups.
Biochem J. 1982 Jul 1;205(1):205-11. doi: 10.1042/bj2050205.
7
Two-protonic-state electrophiles as probes of enzyme mechanisms.
Methods Enzymol. 1982;87:427-69. doi: 10.1016/s0076-6879(82)87026-2.
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Determination of sulfhydryl groups with 2,2'- or 4,4'-dithiodipyridine.
Arch Biochem Biophys. 1967 Mar;119(1):41-9. doi: 10.1016/0003-9861(67)90426-2.
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Anionic proteinase from Actinidia chinensis. Preparation and properties of the crystalline enzyme.
Eur J Biochem. 1970 Jun;14(2):214-21. doi: 10.1111/j.1432-1033.1970.tb00280.x.
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Covalent chromatography. Preparation of fully active papain from dried papaya latex.
Biochem J. 1973 Jul;133(3):573-84. doi: 10.1042/bj1330573.
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