Kinetics of the hydrolysis of N-benzoyl-L-serine methyl ester catalysed by bromelain and by papain. Analysis of modifier mechanisms by lattice nomography, computational methods of parameter evaluation for substrate-activated catalyses and consequences of postulated non-productive binding in bromelain- and papain-catalysed hydrolyses.

A necessary modification to the preparation of papain from any high-quality latex of Carica papaya and evidence for the structural integrity of the enzyme produced by traditional methods. Biochem J (1979) 2.20

Evaluation of rate constants for enzyme-catalysed reactions by the jackknife technique. Application to liver alcohol dehydrogenase. Biochem J (1978) 1.85

Kinetics of rat liver glucokinase. Co-operative interactions with glucose at physiologically significant concentrations. Biochem J (1976) 1.81

Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinase. Biochem J (1977) 1.54

The nature of experimental error in enzyme kinetic measurments. Biochem J (1975) 1.51

Kinetics of nitrogenase of Klebsiella pneumoniae. Heterotropic interactions between magnesium-adenosine 5'-diphosphate and magnesium-adenosine 5'-triphosphate. Biochem J (1977) 1.14

A polyclonal antibody preparation with Michaelian catalytic properties. Biochem J (1991) 1.03

Characterization of the hydrolytic activity of a polyclonal catalytic antibody preparation by pH-dependence and chemical modification studies: evidence for the involvement of Tyr and Arg side chains as hydrogen-bond donors. Biochem J (1997) 0.97

A general kinetic approach to investigation of active-site availability in macromolecular catalysts. Biochem J (2000) 0.87

Kinetic solvent isotope effects on the deacylation of specific acyl-papains. Proton inventory studies on the papain-catalysed hydrolyses of specific ester substrates: analysis of possible transition state structures. Biochem J (1981) 0.84

Polyclonal antibody-catalysed amide hydrolysis. Biochem J (1992) 0.84

Benzyloxycarbonylphenylalanylcitrulline p-nitroanilide as a substrate for papain and other plant cysteine proteinases. Biochem J (1984) 0.80

Evidence for 'lock and key' character in an anti-phosphonate hydrolytic antibody catalytic site augmented by non-reaction centre recognition: variation in substrate selectivity between an anti-phosphonate antibody, an anti-phosphate antibody and two hydrolytic enzymes. Biochem J (2004) 0.80

The structure and mechanism of stem bromelain. Evaluation of the homogeneity of purified stem bromelain, determination of the molecular weight and kinetic analysis of the bromelain-catalysed hydrolysis of N-benzyloxycarbonyl-L-phenylalanyl-L-serine methyl ester. Biochem J (1974) 0.79

Tissue sulfhydryl groups. Arch Biochem Biophys (1959) 61.89

A COMPARISON OF ESTIMATES OF MICHAELIS-MENTEN KINETIC CONSTANTS FROM VARIOUS LINEAR TRANSFORMATIONS. J Biol Chem (1965) 11.92

Application of a Theory of Enzyme Specificity to Protein Synthesis. Proc Natl Acad Sci U S A (1958) 9.18

Mapping the active site of papain with the aid of peptide substrates and inhibitors. Philos Trans R Soc Lond B Biol Sci (1970) 3.29

Negatively co-operative ligand binding. Biochem J (1973) 2.36

PAPAIN-CATALYSED HYDROLYSIS OF SOME HIPPURIC ESTERS. A NEW MECHANISM FOR PAPAIN-CATALYSED HYDROLYSIS. Biochem J (1965) 2.28

KINETICS OF PAPAIN-CATALYZED HYDROLYSIS OF ALPHA-N-BENZOYL-L-ARGININE ETHYL ESTER AND ALPHA-N-BENZOYL-L-ARGININAMIDE. J Am Chem Soc (1965) 2.13

SUBSTRATE ACTIVATION OF TRYPSIN. Biochemistry (1964) 2.09

STUDIES ON THE ACTIVE CENTER OF TRYPSIN. THE BINDING OF AMIDINES AND GUANIDINES AS MODELS OF THE SUBSTRATE SIDE CHAIN. J Biol Chem (1965) 1.92

Phenolic hydroxyl ionization in papain. J Biol Chem (1961) 1.81

The mutability of stem bromelain: evidence for perturbation by structural transitions of the parameters that characterize the reaction of the essential thiol group of bromelain with 2,2'-dipyridyl disulphide. Biochem J (1972) 1.42

A general method for the quantitative determination of saturation curves for multisubunit proteins. Biochemistry (1970) 1.26

The preparation and some properties of bromelain covalently attached to O-(carboxymethyl)-cellulose. Eur J Biochem (1968) 1.22

PREPARATION AND CHEMICAL PROPERTIES OF PURIFIED STEM AND FRUIT BROMELAINS. Biochemistry (1964) 1.21

The rate-limiting reaction in papain action as derived from the reaction of the enzyme with chloroacetic acid. Biochim Biophys Acta (1968) 1.11

Substrate activation of trypsin and acetyltrypsin caused by -N-benzoyl-L-arginine p-nitroanilide. J Biochem (1972) 1.09

PURIFICATION AND PHYSICAL CHARACTERIZATION OF STEM BROMELAIN. Biochemistry (1964) 1.08

The kinetic analysis of hydrolytic enzyme catalyses: Consequences of non-productive binding. FEBS Lett (1968) 1.05

The nature of the perturbation of the michaelis constant of the bromelain-catalysed hydrolysis of alpha-N-benzoyl-L-arginine ethyl ester consequent upon attachment of bromelain to O-(carboxymethyl)-cellulose. Eur J Biochem (1968) 1.05

KINETIC STUDIES OF BROMELAIN CATALYSIS. Biochemistry (1964) 1.01

Kinetics of papain-catalyzed hydrolyses of neutral substrates. Biochemistry (1967) 0.96

Sequence of amino acids in the vicinity of the reactive thiol group of stem bromelain. Biochem Biophys Res Commun (1967) 0.95

ON THE MOLECULAR WEIGHTS OF THE PROTEOLYTIC ENZYMES OF STEM BROMELAIN. Biochemistry (1964) 0.93

THE MECHANISM OF THE SPECIFICITY OF TRYPSIN CATALYSIS. 3. ACTIVATION OF THE CATALYTIC SITE OF TRYPSIN BY ALKYLAMMONIUM IONS IN THE HYDROLYSIS OF ACETYLGLYCINE ETHYL ESTER. J Biol Chem (1964) 0.90

The alpha-chymotrypsin catalyzed hydrolysis of a series of acylated glycine methyl esters. Biochemistry (1963) 0.86

A kinetic analysis of the papain-catalyzed hydrolysis of alpha-N-benzoyl-L-citrulline methyl ester. Biochemistry (1967) 0.84

FRACTIONATION AND PARTIAL CHARACTERIZATION OF THE PROTEOLYTIC ENZYMES OF STEM BROMELAIN. Biochemistry (1964) 0.83

Demonstration of a change in the rate-determining step in papain- and ficin-catalyzed acyl-transfer reactions. Biochemistry (1971) 0.83

Multiple molecular forms of stem bromelain. Isolation and characterization of two closely related components, SB1 and SB2. J Biochem (1973) 0.81

Ficin-and papain-catalyzed reactions. Changes in reactivity of the essential sulfhydryl group in the presence of substrates and competitive inhibitors. Biochemistry (1969) 0.78

The systems biology markup language (SBML): a medium for representation and exchange of biochemical network models. Bioinformatics (2003) 32.92

The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters. Biochem J (1974) 14.12

Nomenclature for incompletely specified bases in nucleic acid sequences: recommendations 1984. Nucleic Acids Res (1985) 9.17

Statistical considerations in the estimation of enzyme kinetic parameters by the direct linear plot andother methods. Biochem J (1974) 6.04

A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem J (1974) 4.52

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) 3.33

A reporter group delivery system with both absolute and selective specificity for thiol groups and an improved fluorescent probe containing the 7-nitrobenzo-2-oxa-1,3-diazole moiety. Biochem J (1975) 3.17

Covalent chromatography. Preparation of fully active papain from dried papaya latex. Biochem J (1973) 2.79

Concentration of MgATP2- and other ions in solution. Calculation of the true concentrations of species present in mixtures of associating ions. Biochem J (1976) 2.75

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 occasioned by its interaction with the histidine-159-asparagine-175 hydrogen-bonded system. Biochem J (1972) 2.65

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) 2.53

The kinetics of coupled enzyme reactions. Applications to the assay of glucokinase, with glucose 6-phosphate dehydrogenase as coupling enzyme. Biochem J (1974) 2.43

Estimation of Michaelis constant and maximum velocity from the direct linear plot. Biochim Biophys Acta (1978) 2.32

A necessary modification to the preparation of papain from any high-quality latex of Carica papaya and evidence for the structural integrity of the enzyme produced by traditional methods. Biochem J (1979) 2.20

The use of the direct linear plot for determining initial velocities. Biochem J (1975) 2.16

Half-time analysis of the integrated Michaelis equation. Simulation and use of the half-time plot and its direct linear variant in the analysis of some alpha-chymotrypsin, papain- and fumarase-catalysed reactions. Biochem J (1982) 2.15

Specific covalent modification of thiols: applications in the study of enzymes and other biomolecules. Int J Biochem (1979) 2.11

Diagnostic uses of the Hill (Logit and Nernst) plots. J Mol Biol (1975) 2.09

PH-dependence of the steady-state rate of a two-step enzymic reaction. Biochem J (1976) 2.08

The effect of natural selection on enzymic catalysis. J Mol Biol (1976) 2.04

Estimation of the dissociation constants of enzyme-substrate complexes from steady-state measurements. Interpretation of pH-independence of Km. Biochem J (1976) 1.91

On arginase and its participation in urea synthesis in the liver. Biochem J (1944) 1.86

Evaluation of rate constants for enzyme-catalysed reactions by the jackknife technique. Application to liver alcohol dehydrogenase. Biochem J (1978) 1.85

The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions. Biochem J (1979) 1.82

Kinetics of rat liver glucokinase. Co-operative interactions with glucose at physiologically significant concentrations. Biochem J (1976) 1.81

4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole as a reactivity probe for the investigation of the thiol proteinases. evidence that ficin and bromelain may lack carboxyl groups conformationally equivalent to that of aspartic acid-158 of papain. Biochem J (1976) 1.77

The pH-dependence of second-order rate constants of enzyme modification may provide free-reactant pKa values. Biochem J (1977) 1.73

Two-protonic-state electrophiles as probes of enzyme mechanisms. Methods Enzymol (1982) 1.70

Covalent chromatography by thiol-disulfide interchange. Methods Enzymol (1974) 1.61

The preparation and properties of ficin chemically attached to carboxymethylcellulose. Biochem J (1966) 1.61

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) 1.60

An automatic method for deriving steady-state rate equations. Biochem J (1977) 1.57

Kinetic evidence for a 'mnemonical' mechanism for rat liver glucokinase. Biochem J (1977) 1.54

A critical analysis of the use of radiation inactivation to measure the mass of protein. Radiat Res (1995) 1.52

A spectrophotometric method for the detection of contaminant chymopapains in preparations of papain. Selective modification of one type of thiol group in the chymopapains by a two-protonic-state reagent. Biochem J (1978) 1.52

Kinetics of the reversible reaction of papain with 5,5'-dithiobis-(2-nitrobenzoate) dianion: evidence for nucleophilic reactivity in the un-ionized thiol group of cysteine-25 and for general acid catalysis by histidine-159 of the reaction of the 5-mercapto-2-nitrobenzoate dianion with the papain-5-mercapto-2-nitrobenzoate mixed disulphide. Biochem J (1972) 1.52

Regulating the cellular economy of supply and demand. FEBS Lett (2000) 1.52

The nature of experimental error in enzyme kinetic measurments. Biochem J (1975) 1.51

The case for assigning a value of approximately 4 to pKa-i of the essential histidine-cysteine interactive systems of papain, bromelain and ficin. FEBS Lett (1975) 1.50

In defence of the general validity of the Cha method of deriving rate equations. The importance of explicit recognition of the thermodynamic box in enzyme kinetics. Biochem J (1992) 1.45

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) 1.44

Relationships between inhibition constants, inhibitor concentrations for 50% inhibition and types of inhibition: new ways of analysing data. Biochem J (2001) 1.44

Purification and properties of nitrite reductase from Escherichia coli K12. Biochem J (1978) 1.43

Assessment of protein sequence identity from amino acid composition data. J Theor Biol (1977) 1.43

Evolution and regulatory role of the hexokinases. Biochim Biophys Acta (1998) 1.43

How reliably do amino acid composition comparisons predict sequence similarities between proteins? J Theor Biol (1979) 1.42

The mutability of stem bromelain: evidence for perturbation by structural transitions of the parameters that characterize the reaction of the essential thiol group of bromelain with 2,2'-dipyridyl disulphide. Biochem J (1972) 1.42

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) 1.39

Relating proteins by amino acid composition. Methods Enzymol (1983) 1.39

Why is uncompetitive inhibition so rare? A possible explanation, with implications for the design of drugs and pesticides. FEBS Lett (1986) 1.38

Critical values for testing the significance of amino acid composition indexes. Anal Biochem (1980) 1.37

The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A. Biochemistry (1993) 1.36

A re-evaluation of the nomenclature of the cysteine proteinases of Carica papaya and a rational basis for their identification. Biochem J (1983) 1.35

The number of catalytic sites in creatine phosphokinase as determined by a study of its reactive sulphydryl groups. Biochem J (1962) 1.33

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) 1.31

Benzofuroxan as a thiol-specific reactivity probe. Kinetics of its reactions with papain, ficin, bromelain and low-molecular-weight thiols. Biochem J (1977) 1.31

The reversible Hill equation: how to incorporate cooperative enzymes into metabolic models. Comput Appl Biosci (1997) 1.30

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) 1.30

The purification in high yield and characterization of rat hepatic glucokinase. Biochem J (1976) 1.29

Evaluation of distribution-free confidence limits for enzyme kinetic parameters. J Theor Biol (1978) 1.27

A general method for the quantitative determination of saturation curves for multisubunit proteins. Biochemistry (1970) 1.26

A classical enzyme active center motif lacks catalytic competence until modulated electrostatically. Biochemistry (1997) 1.26

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) 1.26

The reaction of papain with Ellman's reagent (5,5'-dithiobis- (2-nitrobenzoate) dianion). Biochem J (1972) 1.25

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 papain catalytic mechanism. Biochem J (1978) 1.24

Co-operative and allosteric enzymes: 20 years on. Eur J Biochem (1987) 1.24

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) 1.24

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) 1.23

The preparation and some properties of bromelain covalently attached to O-(carboxymethyl)-cellulose. Eur J Biochem (1968) 1.22

Prosthetic groups of the NADH-dependent nitrite reductase from Escherichia coli K12. Biochem J (1981) 1.22

Consequences of molecular recognition in the S1-S2 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 P1-P2 amide bond into a two-protonic-state reactivity probe. Biochem J (1988) 1.22

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) 1.21

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) 1.19

Fitting of enzyme kinetic data without prior knowledge of weights. Biochem J (1981) 1.19

Effects of conformational selectivity and of overlapping kinetically influential ionizations on the characteristics of pH-dependent enzyme kinetics. Implications of free-enzyme pKa variability in reactions of papain for its catalytic mechanism. Biochem J (1983) 1.19

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) 1.19

Immobilization of urease by thiol-disulphide interchange with concomitant purification. Eur J Biochem (1974) 1.19

A convenient method of preparation of high-activity urease from Canavalia ensiformis by covalent chromatography and an investigation of its thiol groups with 2,2'-dipyridyl disulphide as a thiol titrant and reactivity probe. Biochem J (1976) 1.19

Evaluation of benzofuroxan as a chromophoric oxidizing agent for thiol groups by using its reactions with papain, ficin, bromelain and low-molecular-weight thiols. Biochem J (1977) 1.18

Propapain and its conversion to papain: a new type of zymogen activation mechanism involving intramolecular thiol-disulphide interchange. Nat New Biol (1973) 1.17

The kinetics of carboxymethylcellulose--ficin in packed beds. Biochem J (1966) 1.16

Enzyme specificity: its meaning in the general case. J Theor Biol (1984) 1.15

Algebraic methods for deriving steady-state rate equations. Practical difficulties with mechanisms that contain repeated rate constants. Biochem J (1976) 1.15

Kinetics of nitrogenase of Klebsiella pneumoniae. Heterotropic interactions between magnesium-adenosine 5'-diphosphate and magnesium-adenosine 5'-triphosphate. Biochem J (1977) 1.14

Quantitative assessment of regulation in metabolic systems. Eur J Biochem (1991) 1.13

Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase omega. Biochem J (1985) 1.12

The pre-eminence of k(cat) in the manifestation of optimal enzymic activity delineated by using the Briggs-Haldane two-step irreversible kinetic model. Biochem J (1976) 1.12

Activation of nitrite reductase from Escherichia coli K12 by oxidized nicotinamide-adenine dinucleotide. Biochem J (1978) 1.12

Hydrogen-bonding in enzyme catalysis. Fourier-transform infrared detection of ground-state electronic strain in acyl-chymotrypsins and analysis of the kinetic consequences. Biochem J (1990) 1.11

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) 1.11

The analysis of kinetic data in biochemistry. A critical evaluation of methods. FEBS Lett (1976) 1.10

Isotope-exchange evidence for an ordered mechanism for rat-liver glucokinase, a monomeric cooperative enzyme. Biochemistry (1981) 1.09

The amino acid compositions of proteins are correlated with their molecular sizes. Biochem J (1983) 1.09