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F Willenbrock
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Articles

The C -terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases

G Murphy, F Willenbrock, R V Ward, M I Cockett, D Eaton, A J P Docherty
Journal: Biochemical Journal
Biochem J (1992) 283 (3): 637–641.
https://doi.org/10.1042/bj2830637
Published: 01 May 1992
View article titled, The C -terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases
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Articles

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

K Brocklehurst, S M Brocklehurst, D Kowlessur, M O'Driscoll, G Patel, E Salih, W Templeton, E Thomas, C M Topham, F Willenbrock
Journal: Biochemical Journal
Biochem J (1988) 256 (2): 543–558.
https://doi.org/10.1042/bj2560543
Published: 01 December 1988
View article titled, Supracrystallographic resolution of interactions contributing to enzyme catalysis by use of natural structural variants and reactivity-probe kinetics
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Articles

Consequences of molecular recognition in the S 1 -S 2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P 1 -P 2 amide bond into a two-protonic-state reactivity probe

K Brocklehurst, D Kowlessur, G Patel, W Templeton, K Quigley, E W Thomas, C W Wharton, F Willenbrock, R J Szawelski
Journal: Biochemical Journal
Biochem J (1988) 250 (3): 761–772.
https://doi.org/10.1042/bj2500761
Published: 15 March 1988
View article titled, Consequences of molecular recognition in the S 1 -S 2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P 1 -P 2 amide bond into a two-protonic-state reactivity probe
Open the PDF for Consequences of molecular recognition in the S 1 -S 2 intersubsite region of papain for catalytic-site chemistry. Change in pH-dependence characteristics and generation of an inverse solvent kinetic isotope effect by introduction of a P 1 -P 2 amide bond into a two-protonic-state reactivity probe in another window
Articles

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

K Brocklehurst, D Kowlessur, M O'Driscoll, G Patel, S Quenby, E Salih, W Templeton, E W Thomas, F Willenbrock
Journal: Biochemical Journal
Biochem J (1987) 244 (1): 173–181.
https://doi.org/10.1042/bj2440173
Published: 15 May 1987
View article titled, Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding
Open the PDF for Substrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bonding in another window
Articles

Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites

F Willenbrock, K Brocklehurst
Journal: Biochemical Journal
Biochem J (1986) 238 (1): 103–107.
https://doi.org/10.1042/bj2380103
Published: 15 August 1986
View article titled, Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites
Open the PDF for Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites in another window
Articles

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

F Willenbrock, K Brocklehurst
Journal: Biochemical Journal
Biochem J (1985) 227 (2): 511–519.
https://doi.org/10.1042/bj2270511
Published: 15 April 1985
View article titled, 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
Open the PDF for 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 in another window
Articles

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-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide catalysed by cathepsin B and of l-arginine 2-naphthylamide catalysed by cathepsin H.

F Willenbrock, K Brocklehurst
Journal: Biochemical Journal
Biochem J (1985) 227 (2): 521–528.
https://doi.org/10.1042/bj2270521
Published: 15 April 1985
View article titled, 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-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide catalysed by cathepsin B and of l-arginine 2-naphthylamide catalysed by cathepsin H.
Open the PDF for 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-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide catalysed by cathepsin B and of l-arginine 2-naphthylamide catalysed by cathepsin H. in another window
Articles

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-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide)

F Willenbrock, K Brocklehurst
Journal: Biochemical Journal
Biochem J (1984) 222 (3): 805–814.
https://doi.org/10.1042/bj2220805
Published: 15 September 1984
View article titled, 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-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide)
Open the PDF for 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-α-benzyloxycarbonyl-l-arginyl-l-arginine 2-naphthylamide) in another window
Articles

Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme p K a variability in reactions of papain for its catalytic mechanism

K Brocklehurst, S J F Willenbrock, E Salih
Journal: Biochemical Journal
Biochem J (1983) 211 (3): 701–708.
https://doi.org/10.1042/bj2110701
Published: 01 June 1983
View article titled, Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme p K a variability in reactions of papain for its catalytic mechanism
Open the PDF for Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme p K a variability in reactions of papain for its catalytic mechanism in another window
Articles

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

K Brocklehurst, S M Mushiri, G Patel, F Willenbrock
Journal: Biochemical Journal
Biochem J (1983) 209 (3): 873–879.
https://doi.org/10.1042/bj2090873
Published: 01 March 1983
View article titled, 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
Open the PDF for 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 in another window
Articles

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

K Brocklehurst, S M Mushiri, G Patel, F Willenbrock
Journal: Biochemical Journal
Biochem J (1982) 201 (1): 101–104.
https://doi.org/10.1042/bj2010101
Published: 01 January 1982
View article titled, 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
Open the PDF for 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 in another window