(Q28356754)

English

The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain

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scholarly article

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The interplay of electrostatic fields and binding interactions determining catalytic-site reactivity in actinidin. A possible origin of differences in the behaviour of actinidin and papain (English)

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author name string

D Kowlessur

1

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M O'Driscoll

2

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C M Topham

3

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W Templeton

4

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E W Thomas

5

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K Brocklehurst

6

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language of work or name

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publication date

15 April 1989

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Biochemical Journal

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259

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443-52

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2

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Thiol proteases. Comparative studies based on the high-resolution structures of papain and actinidin, and on amino acid sequence information for cathepsins B and H, and stem bromelain

1 reference

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20 March 2017

Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding

1 reference

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20 March 2017

Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics

1 reference

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20 March 2017

1 reference

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20 March 2017

Dependence of the catalytic activity of papain on the ionization of two acidic groups

1 reference

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20 March 2017

Mapping the active site of papain with the aid of peptide substrates and inhibitors

1 reference

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29 September 2017

Crystallographic studies of the activity of hen egg-white lysozyme

1 reference

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29 September 2017

The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis

1 reference

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29 September 2017

The case for assigning a value of approximately 4 to pKaI of the essential histidine-cysteine interactive systems of papain, bromelain and ficin

1 reference

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29 September 2017

Mechanism of thiol protease catalysis: detection and stabilization of a tetrahedral intermediate in papain catalysis

1 reference

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29 September 2017

Intramolecular Inhibition by Enzyme of Site-Specific Modification Reactions can Mask pKa Values Characteristic of the Reaction Pathway: Do the Side Chains of Aspartic Acid-158 and Lysine-156 of Papain Form an Ion-Pair?

1 reference

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29 September 2017

The organization and function of water in protein crystals

1 reference

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29 September 2017

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

1 reference

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29 September 2017

Appendix: Analysis of pH-dependent kinetics in up to four reactive hydronic states

1 reference

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2 June 2018

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 reac

1 reference

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2 June 2018

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

1 reference

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2 June 2018

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.

1 reference

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2 June 2018

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 di

1 reference

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2 June 2018

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, pK

1 reference

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2 June 2018

Kinetic specificity in papain-catalysed hydrolyses

1 reference

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2 June 2018

Reactivities of the various protonic states in the reactions of papain and of L-cysteine with 2,2'- and with 4,4'- dipyridyl disulphide: evidence for nucleophilic reactivity in the un-ionized thiol group of the cysteine-25 residue of papain occasion

1 reference

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2 June 2018

Benzoylamidoacetonitrile as an inhibitor of papain

1 reference

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2 June 2018

The electrostatic fields in the active-site clefts of actinidin and papain

1 reference

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2 June 2018

Structural and electrostatic differences between actinidin and papain account for differences in activity

1 reference

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2 June 2018

The interplay of electrostatic and binding interactions determining active centre chemistry and catalytic activity in actinidin and papain

1 reference

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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 stu

1 reference

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Mechanism of the reaction of papain with substrate-derived diazomethyl ketones. Implications for the difference in site specificity of halomethyl ketones for serine proteinases and cysteine proteinases and for stereoelectronic requirements in the pa

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Mechanism of action of papain with a specific anilide substrate

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2 June 2018

Cloning and sequencing of papain-encoding cDNA.

1 reference

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A novel reactivity of papain and a convenient active site titration in the presence of other thiols

1 reference

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A nuclear magnetic resonance study of enzyme-inhibitor association. The use of pH and temperature effects to probe the binding environments

1 reference

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Ionization behavior of the catalytic carboxyls of lysozyme

1 reference

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Structure of actinidin, after refinement at 1.7 A resolution

1 reference

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Cryoenzymology of papain: reaction mechanism with an ester substrate

1 reference

https://pubmed.ncbi.nlm.nih.gov/2719659

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Anionic Proteinase from Actinidia chinensis. Preparation and Properties of the Crystalline Enzyme

1 reference

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A rapid method of calculating charge-charge interaction energies in proteins

1 reference

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Identifiers

10.1042/BJ2590443

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