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(RS)-mandelic hydrazide + benzyloxycarbonyl-Ala
N1-(benzyloxycarbonyl-Ala)-N2-[(R)-mandelyl]hydrazine + N1-(benzyloxycarbonyl-Ala)-N2-[(S)-mandelyl]hydrazine
-
-
mixture of diastereoisomers containing 73% N1-(benzyloxycarbonyl-Ala)-N2-[(R)-mandelyl]hydrazine
?
(RS)-mandelic hydrazide + benzyloxycarbonyl-Gly
N1-(benzyloxycarbonyl-Gly)-N2-[(R)-mandelyl]hydrazine + N1-(benzyloxycarbonyl-Gly)-N2-[(S)-mandelyl]hydrazine
-
-
-
?
(RS)-mandelic hydrazide + hippuric acid
?
-
-
-
-
?
(RS)-mandelic hydrazide + N(tert-amyloxycarbonyl)-Gly
(+)-N1-(tert-amyloxycarbonyl-Gly)-NH2-[(R)-mandelyl]hydrazine + N1-(tert-butoxycarbonyl-Gly)-N2-[(S)-mandelyl]hydrazine
-
-
-
?
(RS)-mandelic hydrazide + N-(tert-butyloxycarbonyl)-Gly
(+)-N1-(tert-butyloxycarbonyl-Gly)-N2[(R)-mandelyl]hydrazine + (+)-(N1)-(tert-butyloxycarbonyl-Gly)-N2[(S)-mandelyl]hydrazine
-
-
-
-
?
2-(amino)ethyl 2'-pyridyl disulfide + H2O
?
-
-
-
-
?
3-(amino)trimethylene 2'-pyridyl disulfide + H2O
?
-
-
-
-
?
4-(amino)-tetramethylene 2'-pyridyl disulfide + H2O
?
-
-
-
-
?
Ac-L-Phe-Gly 4-nitroanilide + H2O
Ac-L-Phe-Gly + 4-nitroaniline
-
whole hydrolysis process includes two stages: acylation and deacylation. The first step is a proton transfer to form a zwitterionic form (i.e. Cys-S-/His-H+ion-pair), and the second step is the nucleophilic attack on the carboxyl carbon of the substrate accompanied with the dissociation of 4-nitroaniline. The deacylation stage includes the nucleophilic attack of a water molecule on the carboxyl carbon of the substrate and dissociation between the carboxyl carbon of the substrate and the sulfhydryl sulfur of Cys25 side chain. The acylation is rate-limiting
-
-
?
acetyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
-
-
-
?
acetyl-L-Phe-Gly-4-nitroanilide + H2O
acetyl-L-Phe-Gly + 4-nitroaniline
-
-
-
-
?
alpha-lactalbumin + H2O
?
-
-
-
-
?
alpha-N-benzoyl-DL-Arg-p-nitroanilide + H2O
?
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
azocasein + H2O
azopeptide + peptides
-
-
-
?
benzaldehyde + acetylacetone
3-benzylidenepentane-2,4-dione
-
35% yield after 72 h at 25°C or 55% yield after 81 h at 60°C. 150 mg of papain is the optimum quantity for the Knoevenagel reaction between 2 mM of benzaldehyde and 2.4 mM of acetylacetone in 5 ml of DMSO/H2O
-
-
?
benzoyl arginine ethyl ester + H2O
?
-
pH 6.3, 20°C
-
-
?
benzoyl-L-Arg-2-naphthylamide + H2O
benzoyl-L-Arg + 2-naphthylamine
-
-
-
-
?
benzoyl-thiocarbamic acid + H2O
N-benzoyl-Gly + SH2
-
-
-
-
?
benzoyl-thiocarbamic acid ethyl ester + H2O
N-benzoyl-Gly + ethanethiol
-
-
-
-
?
benzoyl-thiocarbamic acid methyl ester + H2O
N-benzoyl thioglycine + methanol
-
-
-
-
?
benzyl-Phe-Val-Arg-4-nitroanilide + H2O
benzyl-Phe-Val-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ala methyl ester + L-Arg
benzyloxycarbonyl-Ala-Arg-OH
-
-
-
?
benzyloxycarbonyl-Ala-Arg-NH2 + Arg-NH2
benzyloxycarbonyl-Ala-Arg-Arg-NH2
-
-
-
?
benzyloxycarbonyl-Ala-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Ala-4-aminoantipyrine + methanol
-
-
-
?
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Gly-4-aminoantipyrine + methanol
-
-
-
?
benzyloxycarbonyl-L-citrullyl-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-citrullyl-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin + H2O
benzyloxycarbonyl-L-Phe-L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Phe-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu-4-nitroanilide + H2O
benzyloxycarbonyl-Phe-Leu + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Ser-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Ser-4-aminoantipyrine + methanol
-
-
-
?
beta-lactoglobulin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
carboxybenzoyl-Phe-Arg-7-(4-methyl)coumarylamide + H2O
carboxybenzoyl-Phe-Arg + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
casein + H2O
L-tyrosine + ?
-
-
-
-
?
CBZ-beta-Ala 4-guanidinophenyl ester + L-Phe-NH2 + H2O
CBZ-beta-Ala-L-Phe-NH2 + CBZ-beta-Ala + 4-guanidinophenol
-
-
31.6% yield of CBZ-beta-Ala-L-Phe-NH2
-
?
CBZ-D-Ala 4-guanidinophenyl ester + L-Phe-NH2 + H2O
CBZ-D-Ala-L-Phe-NH2 + CBZ-D-Ala + 4-guanidinophenol
-
-
11.6% yield of CBZ-D-Ala-L-Phe-NH2
-
?
CBZ-Gly 4-guanidinophenyl ester + D-Phe-NH2 + H2O
CBZ-Gly-D-Phe-NH2 + CBZ-Gly + 4-guanidinophenol
-
-
22.9% yield for CBZ-Gly-D-Phe-NH2 and 74.3% yield for CBZ-Gly
-
?
CBZ-Gly 4-guanidinophenyl ester + H2O
CBZ-Gly + 4-guanidinophenol
-
-
94.8% yield for CBZ-Gly
-
?
CBZ-Gly 4-guanidinophenyl ester + L-Ala 4-nitroanilide + H2O
CBZ-Gly-L-Ala 4-nitroanilide + CBZ-Gly + 4-guanidinophenol
-
-
96% yield for CBZ-Gly-L-Ala 4-nitroanilide
-
?
CBZ-Gly 4-guanidinophenyl ester + L-Ala-NH2 + H2O
CBZ-Gly-L-Ala-NH2 + CBZ-Gly + 4-guanidinophenol
-
-
87% yield for Gly-L-Ala-NH2 and 7.7% yield for Gly-OH
-
?
CBZ-Gly 4-guanidinophenyl ester + L-Phe tert-butyl ester + H2O
CBZ-Gly-L-Phe tert-butyl ester + CBZ-Gly + 4-guanidinophenol
-
-
11.8% yield for CBZ-Gly-L-Phe tert-butyl ester
-
?
CBZ-Gly 4-guanidinophenyl ester + L-Phe-NH2 + H2O
CBZ-Gly-L-Phe-NH2 + CBZ-Gly + 4-guanidinophenol
-
-
92% yield of CBZ-Gly-L-Phe-NH2
-
?
CBZ-Gly 4-guanidinophenyl ester + L-Pro 4-nitroanilide + H2O
CBZ-Gly-L-Pro 4-nitroanilide + CBZ-Gly + 4-guanidinophenol
-
-
90.3% yield for CBZ-Gly
-
?
CBZ-Gly 4-guanidinophenyl ester + L-Ser 4-nitroanilide + H2O
CBZ-Gly-L-Ser 4-nitroanilide + CBZ-Gly + 4-guanidinophenol
-
-
94% yield for CBZ-Gly-L-Ser 4-nitroanilide
-
?
CBZ-Gly 4-guanidinophenyl ester + L-Tyr 4-nitroanilide + H2O
CBZ-Gly-L-Tyr 4-nitroanilide + CBZ-Gly + 4-guanidinophenol
-
-
90.6% yield for CBZ-Gly-L-Tyr 4-nitroanilide and 4.3% yield for CBZ-Gly
-
?
CBZ-Gly 4-guanidinophenyl ester + L-Tyr-NH2 + H2O
CBZ-Gly-L-Tyr-NH2 + CBZ-Gly + 4-guanidinophenol
-
-
91.3% yield for CBZ-Gly-L-Tyr-NH2 and 2.5% yield for CBZ-Gly
-
?
CBZ-L-Ala 4-guanidinophenyl ester + L-Phe-NH2 + H2O
CBZ-L-Ala-L-Phe-NH2 + CBZ-L-Ala + 4-guanidinophenol
-
-
77.5% yield of CBZ-L-Ala-L-Phe-NH2
-
?
CBZ-L-Arg 4-guanidinophenyl ester + L-Phe-NH2 + H2O
CBZ-L-Arg-L-Phe-NH2 + CBZ-L-Arg + 4-guanidinophenol
-
-
45.9% yield of CBZ-L-Arg-L-Phe-NH2
-
?
CBZ-L-Asn 4-guanidinophenyl ester + L-Phe-NH2 + H2O
L-Asn-L-Phe-NH2 + CBZ-L-Asn + 4-guanidinophenol
-
-
6.1% yield of CBZ-L-Asn-L-Phe-NH2
-
?
CBZ-L-Glu 4-guanidinophenyl ester + L-Phe-NH2 + H2O
CBZ-Glu-L-Phe-NH2 + CBZ-L-Glu + 4-guanidinophenol
-
-
68.5% yield of CBZ-L-Glu-L-Phe-NH2
-
?
CBZ-L-Ile 4-guanidinophenyl ester + L-Phe-NH2 + H2O
CBZ-L-Ile-L-Phe-NH2 + CBZ-L-Ile + 4-guanidinophenol
-
-
24.5% yield of CBZ-L-Ile-L-Phe-NH2
-
?
CBZ-L-Thr 4-guanidinophenyl ester + L-Phe-NH2 + H2O
CBZ-L-Thr-L-Phe-NH2 + CBZ-L-Thr + 4-guanidinophenol
-
-
90.7% yield of CBZ-L-Thr-L-Phe-NH2
-
?
CH3-CH2-2-pyridyl disulfide + H2O
?
-
-
-
-
?
CH3CO-(D-Phe)-NH-[CH2]2-2-pyridyl disulfide + H2O
?
-
-
-
-
?
CH3CO-(D-Phe)-O-[CH2]2-2-pyridyl disulfide + H2O
?
-
-
-
-
?
CH3CO-(L-Phe)-NH-[CH2]2-2-pyridyl disulfide + H2O
?
-
-
-
-
?
CH3CO-(L-Phe)-O-[CH2]2-2-pyridyl disulfide + H2O
?
-
-
-
-
?
CH3CO-NH-[CH2]2-2-pyridyl disulfide + H2O
?
-
-
-
-
?
CH3CO-O-[CH2]2-2-pyridyl disulfide + H2O
?
-
-
-
-
?
chicken IgY + H2O
?
-
-
-
-
?
chitosan + H2O
low molecular weight chitosan + ?
the enzymolysis process is analyzed using pseudo-first-order and pseudo-second-order kinetic models and the experiment data are more consistent with the pseudo-second-order kinetic model. The Haldane kinetic model adequately describes the dynamic behavior of the chitosan enzymolysis by papain. When the initial chitosan concentration is above 8.0 g/l, the papain is overloaded and exhibits significant inhibition
-
-
?
chitosan + H2O
low-molecular mass chitosan + chito-oligomeric-monomeric mixture
CopA + H2O
?
-
CopA is a bacterial Cu+-ATPase from Thermotoga maritima and contains 3 papain cleavage sites on the C-terminal side of the N-terminal metal binding domain
-
-
?
cucurbitin + H2O
?
-
the reaction occurs in two successive steps. In the first step, limited proteolysis consisting of detachments of short terminal peptides from the alpha and beta chains are observed. The cooperative proteolysis, which occurs as a pseudo-first order reaction, started at the second step. The limited proteolysis at the first step plays a regulatory role, impacting the rate of deep degradation of cucurbitin molecules by the cooperative mechanism
-
-
?
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans + H2O
Dabcyl-Lys-Phe-Gly + Gly-Ala-Ala-Edans
DL-4-hydroxyphenylglycine methyl ester + H2O
?
-
asymmetric hydrolysis
-
-
?
fibroin + H2O
?
-
-
upon papain hydrolysis of fibroin composed of highly repetitive Ala- and Gly-rich blocks even-numbered peptides are obtained. The even-numbered peptides are in the forms of di-, tetra-, hexa-, and octa-peptides with repeating units in combination of Ala-Gly, Ser-Gly, Tyr-Gly, and Val-Gly. The sequences of the tetra-peptides are in the order of Ala-Gly-X-Gly, where X is Tyr or Val
-
?
fish IgM + H2O
?
-
-
-
-
?
Glucagon + H2O
?
-
-
-
-
?
Hemoglobin + H2O
?
-
alpha-chain and beta-chain
-
-
?
hippuric acid + aniline
hippuryl anilide
-
weak activity, 0.1% of the hydrolytic activity with N-benzoyl-L-argininamide
-
r
human IgG + H2O
fragment Fab + fragment Fc
-
-
-
?
immunoglobulin M + H2O
IgMI +
-
release of a basic subunit-like fragment which is designated IgMI, by proteolysis of the mü-chain near the carboxyl terminus
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
L-glutamic acid diethyl ester + L-glutamic acid diethyl ester
L-Glu-gamma-diethyl ester polymer
-
polymerization reaction
-
-
?
L-glutamic acid diethyl ester + L-glutamic acid diethyl ester
oligo-gamma-ethyl-L-glutamate
-
oligomerization reaction
-
-
?
L-glutamic acid diethyl ester + N-alpha-benzoyl-L-arginine ethyl ester
N-alpha-benzoyl-L-argininyl-L-glutamte-diethyl ester + ethanol
-
-
-
-
?
L-glutamic acid triethyl ester + N-alpha-benzoyl-L-arginine ethyl ester
N-alpha-benzoyl-L-arginine + N-alpha-benzoyl-L-argininyl-Glu-Glu-triethyl ester
-
L-glutamic acid triethyl ester shows higher affinity for papain than L-glutamic acid diethyl ester
-
-
?
L-phenylalanine amide + H2O
L-phenylalanine + NH3
-
-
-
-
?
L-Pro-L-Phe-L-Leu-4-nitroanilide + H2O
L-Pro-L-Phe-L-Leu + 4-nitroaniline
-
-
-
-
?
L-Pro-Phe-Leu-4-nitroanilide + H2O
L-Pro-Phe-Leu + 4-nitroaniline
-
-
-
-
?
lambda repressor + H2O
?
-
no cleavage of the operator-bound repressor dimer
-
?
lipid transfer protein + H2O
?
-
-
-
-
?
low molecular weight heparin + H2O
?
-
-
-
-
?
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2 + H2O
?
-
pH 6.2 or pH 7.4, 10 min, 37°C
-
-
?
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2 + H2O
methyl red-Abu-Ala-Pro-Val-Lys + Lys(N5-(5-carboxyfluorescein))-NH2
-
FRET 2, fluorescence resonance energy transfer peptide 2
-
-
?
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N5-(5-carboxyfluorescein))-NH2 + H2O
?
-
pH 6.2 or pH 7.4, 10 min, 37°C
-
-
?
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2 + H2O
methyl red-Abu-Ser-Ala-Pro-Val-Lys + Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
FRET 1, fluorescence resonance energy transfer peptide 1
-
-
?
N(beta-phenylpropionyl)Gly methyl ester + H2O
?
-
-
-
-
?
N,N-diBoc-dityrosine-(isoniazid)2 + H2O
?
-
-
-
-
?
N-(beta-phenylpropionyl)Gly methyl thiono ester + H2O
?
-
-
-
-
?
N-acetyl-L-Trp p-nitrophenyl ester + H2O
?
-
-
-
-
?
N-acetyl-L-tyrosinamide + H2O
N-acetyl-L-Tyr + NH3
-
-
-
-
?
N-alpha-benzoyl-DL-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester + H2O
?
-
-
-
-
?
N-benzoyl-Arg-p-nitroanilide + H2O
Nalpha-benzoyl-Arg + p-nitroaniline
-
-
-
?
N-benzoyl-DL-arginine-2-naphthylamide + H2O
N-benzoyl-DL-arginine + 2-naphthylamine
-
-
-
-
?
N-benzoyl-Gly ethyl ester + H2O
N-benzoyl-Gly + ethanol
-
-
-
-
?
N-benzoyl-Gly methyl ester + H2O
?
-
-
-
-
?
N-benzoyl-Gly methyl ester + H2O
N-benzoyl-Gly + methanol
-
-
-
-
?
N-benzoyl-Gly methyl thiono ester + H2O
?
-
-
-
-
?
N-benzoylglycinamide + H2O
Nalpha-benzoyl-Gly + NH3
-
-
-
-
?
N-benzyloxycarbonyl-Ala methyl ester + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly 2-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + 2-nitrophenol
-
-
-
-
?
N-benzyloxycarbonyl-Gly 3-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + 3-nitrophenol
-
-
-
-
?
N-Benzyloxycarbonyl-Gly 4-nitrophenyl ester + H2O
N-Benzyloxycarbonyl-Gly + 4-nitrophenol
-
-
-
-
?
N-benzyloxycarbonyl-Gly ethyl ester + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly phenyl ester + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Gly + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly-p-nitroanilide + H2O
?
-
-
-
?
N-benzyloxycarbonyl-L-Glu diamide + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-L-glycine + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-L-histidinamide + H2O
Nalpha-benzoyl-L-His + NH3
-
-
-
-
?
N-benzyloxycarbonyl-L-leucinamide + H2O
Nalpha-benzoyl-L-Leu + NH3
-
-
-
-
?
N-benzyloxycarbonyl-L-Lys + H2O
?
-
-
-
-
?
n-propyl 2-pyridyl disulfide + H2O
?
-
-
-
-
?
Nalpha-benzoyl-Arg-p-nitroanilide + H2O
Nalpha-benzoyl-Arg + p-nitroaniline
-
-
-
?
Nalpha-benzoyl-DL-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
?
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-Gly methyl ester + H2O
Nalpha-benzoyl-Gly + methanol
-
-
-
-
?
Nalpha-benzoyl-L-Arg ethyl ester
?
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-argininamide + H2O
Nalpha-benzoyl-L-Arg + NH3
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-citrulline methyl ester + H2O
?
-
-
-
-
?
Nalpha-benzoyl-L-lysinamide + H2O
Nalpha-benzoyl-L-Lys + NH3
-
-
-
-
?
Nalpha-benzyloxycarbonyl-L-histidinamide + H2O
?
-
-
-
-
?
ovalbumin + H2O
?
-
-
-
-
?
oxidized beta-chain of insulin + H2O
?
-
-
-
-
?
Phe-Arg-4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
phthalyl-Phe-Leu-p-nitroanilide + H2O
phthalyl-Phe-Leu + 4-nitroaniline
-
-
-
?
rabbit IgG + H2O
?
-
-
-
-
?
sarcoendoplasmic reticulum Ca2+-ATPase 1 + H2O
?
-
-
-
-
?
sheep IgG + H2O
?
-
-
-
-
?
succinyl-Phe-Leu-4-methylcoumaryl-7-amide + H2O
?
-
-
-
?
succinyl-Phe-Leu-4-nitroanilide + H2O
succinyl-Phe-Leu + 4-nitroaniline
-
-
-
-
?
succinyl-Phe-Leu-p-nitroanilide + H2O
?
-
-
-
?
succinyl-Phe-Leu-p-nitrophenol + H2O
?
-
-
-
?
tarocystatin + H2O
?
the C-terminal cystatin-like extension of tarocystatin is easily digested by papain
-
-
?
ubiquitin-7-amido-4-trifluoromethylcoumarin + H2O
?
-
-
-
-
?
Z-Phe-Arg-4-nitroanilide + H2O
Z-Phe-Arg + 4-nitroaniline
-
-
-
-
?
additional information
?
-
casein + H2O
?
-
-
-
-
?
chitosan + H2O
low-molecular mass chitosan + chito-oligomeric-monomeric mixture
-
depolymerization
product analysis by FTIR and NMR spectroscopy, overview
-
?
chitosan + H2O
low-molecular mass chitosan + chito-oligomeric-monomeric mixture
-
depolymerization, the enzyme inhibits the growth of bacteria such as Bacillus cereus strain F4810, Bacillus licheniformis, and Escherichia coli strain D21, mechanism of bactericidal action of the chito-oligomeric-monomeric mixture, overview
-
-
?
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans + H2O
Dabcyl-Lys-Phe-Gly + Gly-Ala-Ala-Edans
-
-
-
?
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans + H2O
Dabcyl-Lys-Phe-Gly + Gly-Ala-Ala-Edans
-
-
-
?
additional information
?
-
-
existence of an acyl-enzyme intermediate
-
-
?
additional information
?
-
-
the enzyme may play a protective role guarding the plant against attack by pests such as insects and fungi
-
-
?
additional information
?
-
-
papain protects papaya trees from herbivorous insects, e.g. lepidoteran larvae of Samia ricini or polyphagous pests Mamestra brassicae and Spodoptera litura, the enzyme is toxic for the insect larvae, overview
-
-
?
additional information
?
-
-
activation reaction of the enzyme with seven different substrate-derived 2-pyridyl disulfide reactivity probes, specificity, overview
-
-
?
additional information
?
-
-
interaction anaylsis of enzyme with diverse synthetic peptides in a phage display assay, overview
-
-
?
additional information
?
-
molecular recognition of mature enzyme and prosegment, overview
-
-
?
additional information
?
-
-
enzyme catalyses the hydrolysis of peptide bonds of basic amino acids, such as leucine or glycine
-
-
?
additional information
?
-
papain is the founding member of the large C1 family of papain-like cysteine proteases
-
-
?
additional information
?
-
-
glycine is not recognized by papain
-
-
?
additional information
?
-
-
papain is also able to synthesize L-aminoacylantipyrine amides, Z-Gly-Phe-NH2 and Boc-Gly-Phe-OMe, and performs hydrogenation of methyl 2-acetamidoacrylate
-
-
?
additional information
?
-
-
interaction between papain and two ionic liquids, 1-octyl-3-methylimidazolium chloride ([C8mim]Cl) and 1-butyl-3-methylimidazolium chloride ([C4mim]Cl), is investigated by using fluorescence spectroscopy technique at a pH value of 7.4. 1-octyl-3-methylimidazolium chloride has a stronger binding ability with papain than 1-butyl-3-methylimidazolium chloride
-
-
?
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(2-[(S,R)-2-oxo-4-phenylazetidin-1-yl]acetyl)-L-phenylalanine methyl ester
-
weak inhibitor, irreversible
(2-[(S,R)-2-oxo-4-phenylazetidin-1-yl]acetyl)-L-Val benzyl ester
-
weak inhibitor, irreversible
(eta5-C5H5)Fe(CO)3 eta1-N-succinimidato
-
metallocarbonyl complex, reversible inhibitor
-
(eta5-C5H5)Mo(CO)3 eta1-N-succinimidato
-
metallocarbonyl complex, reversible inhibitor
-
(eta5-C5H5)W(CO)3 eta1-N-succinimidato
-
metallocarbonyl complex, reversible inhibitor
-
(S)-1-[(S)-N-(tert-butyloxycarbonyl)alanyl]-4-oxoazetidine-2-carboxylic acid
-
weak, irreversible inactivation
(S,R)-1-[(S)-N-(tert-butyloxycarbonyl)alanyl]-4-phenylazetidin-2-one
-
weak inhibitor, irreversible
1,1-dicyano-2-(4,5-dimethoxy-2-nitrophenyl)-ethene
-
irreversible, photosensitive inhibitor
1-(4,5-dimethoxy-2-nitrophenyl)-2-nitroethene
-
irreversible, photosensitive inhibitor
2-Pentanone
-
noncompetitive
acetyl-Phe-Gly-S-nitrosopenicillamine
-
inactivation of papain by S-nitrosothiols is due to a direct attack of the highly reactive thiolate Cys25 in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between the inactivator and papain
barley cystatin protease inhibitor
-
inhibited by various cystatin vatiants, HvCPI-1, HvCPI-2, HvCPI-3, HvCPI-4, HvCPI-5, HvCPI-6
-
benzoylarginine
-
competitive
benzoylglycine
-
competitive
benzyl-(S)-1-[(S)-N-(tert-butyloxycarbonyl)alanyl]-4-oxoazetidine-2-carboxylate
-
weak, irreversible inactivation
benzyl-(S)-2-(benzyloxycarbonyl)azetidin-1-acetate
-
weak, irreversible inactivation
benzyloxycarbonyl-Arg-Leu-Val-Gly-CHN2
-
-
benzyloxycarbonyl-Phe-Ala-glyoxal
-
competitive, 13C-NMR study of the inhibition
carbobenzyloxy-leucinyl-leucinyl-leucinal
-
chitosan
the Haldane kinetic model adequately describes the dynamic behavior of the chitosan enzymolysis by papain. When the initial chitosan concentration is above 8.0 g/l, the papain is overloaded and exhibits significant inhibition
CNWAAGYNCGGGS-NH2
-
synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
CNWTLGGYKCGGGS-NH2
-
synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
Co2+
5 mM, 46% loss of activity (soluble enzyme), 30% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
CpPRI
-
pathogenesis-related class 10 protein with noncompetitive papain inhibitory activity, purified from Crotalaria pallida roots. CpPRI is made up of a single polypeptide chain with a Mr of 15 kDa
-
Cu2+
-
residual activity in the presence of 20 mM: 0% free papain, 20% immobilized papain
CWEWGGWHCGGSS-OH
-
synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
CWSMMGFQCGGGS-NH2
-
weak inhibition, synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
cystatin SN variant G12A/G13A
-
-
-
cystatin SN variant P106G/W107G
-
-
-
cystatin SN variant Y56G/T57G/V58G
-
-
-
diethyldisulfide-beta,beta'-dicarboxylic acid
-
-
dimethyl sulfoxide
-
the number of active sites of papain decreases with increasing concentration of dimethyl sulfoxide whereas the incubation time, in a buffer containing 3% dimethyl sulfoxide does not affect the number of active sites. A rapid decrease of the initial reaction rate, by up to 30%, is observed between 1 and 2% dimethyl sulfoxide
dimethylformamide
-
number of papain active sites decreases with increase of inhibitor concentration
endopin 2
-
highly effective inhibition, cross-class inhibition of papain and elastase. Localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells
-
ethanol
-
activity decreases with increasing ethanol content, up to 15% ethanol papain from papaya latex is less sensitive to ethanol
ethyl-(RS)-2-(2-oxo-4-phenylazetidin-1-yl)acetate
-
weak inhibitor, irreversible
Fe2+
5 mM, 44% loss of activity (soluble enzyme), 32% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
glucose-2S-nitroso-N-acetyl-penicillamine
-
inactivation of papain by S-nitrosothiols is due to a direct attack of the highly reactive thiolate Cys25 in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between the inactivator and papain
GNWTLGGYKGG
-
weak inhibition, synthetic cyclic peptide, cyclization head-to-tail
Hg2+
papain activity increases to a maximum of 111.03% (non-competitive type activation) at a concentration of 0.000001x01mol/l Hg2+, but is almost completely deactivated at concentrations above 0.0001 mol/lx01Hg2+. The inhibition of Hg2+ on papain is a competitive and uncompetitive mixed type inhibition
inhibitor of cysteine protease
-
-
-
kininogen2
-
from bovine, rat or human
-
Kunitz type trypsin inhibitor
-
i.e. PTPKI, SwissProt: P32722 (alpha chain), P32773 (beta-chain), a small Kunitz trypsin inhibitor from Prosopis juliflora, 0.025 mg/ml, 98.3% inhibition, overlapping binding sites for trypsin and papain
-
L-Ala-L-Phe-aminoacetonitrile
-
-
methanol
-
number of papain active sites decreases with increase of inhibitor concentration
methyl methanethiosulfonate
-
-
N-benzyloxycarbonyl-L-Phe-L-Ala chloromethyl ketone
-
-
N-methylcyrhetrene-pyrrole-2,5-dione
-
-
N-methylferrocene-pyrrole-2,5-dione
-
-
N-methylruthenocene-pyrrole-2,5-dione
-
-
N-[N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl]-isoamylamide
-
-
Ni2+
-
residual activity in the presence of 20 mM: 0% free papain, 16% immobilized papain
oryzacastatin
-
and fragments. The NH2-terminal 21 rsidues including Gly5 and the COOH-terminal 11 residues of the inhibitor are not essential for inhibition
-
p-CH3-C6H4(SO2)-NH-CH2-CO-CH2Cl
-
-
papain inhibitors
-
A1, A2, A3, B2 and C from seeds of Vigna unguiculata subsp. cylindrica
-
PdKl-3.1
-
peptide inhibitor purified from seed of Pithecellobium dumosum tree, stable over a wide range of pH and temperature. Inhibitory to trypsin, moderately inhibitory to papain
-
PdKl-3.2
-
peptide inhibitor purified from seed of Pithecellobium dumosum tree, stable over a wide range of pH and temperature. Inhibitory to trypsin, moderately inhibitory to papain
-
S-nitroso-N-acetyl-DL-penicillamine
-
inactivation of papain by S-nitrosothiols is due to a direct attack of the highly reactive thiolate Cys25 in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between the inactivator and papain
S-nitrosocaptopril
-
inactivation of papain by S-nitrosothiols is due to a direct attack of the highly reactive thiolate Cys25 in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between the inactivator and papain
S-nitrosoglutathione
-
inactivation of papain by S-nitrosothiols is due to a direct attack of the highly reactive thiolate Cys25 in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between the inactivator and papain
succinyl-Ala-Val-Val-Ala-Ala-p-nitroanilide
-
-
succinyl-Gln-Val-Val-Ala-Ala methyl ester
-
-
succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide
-
-
succinyl-Gln-Val-Val-Ala-p-nitroanilide
-
-
succinyl-Gln-Val-Val-p-nitroanilide
-
weak inhibition
tarocystatin
the N-terminal cystatin domain (residues 1-98) of tarocystatin has inhibitory ability against papain
-
Urea
-
the reversible unfolding/refolding process of the PLpro in the presence of urea is investigated. The zinc-binding domain of the enzyme starts to unfold at urea concentration below 0.35 M and reaches a first plateau at 1-3.5 M. At this stage, the palm and thumb core domains remain well folded but totally inactive
Ba2+
-
residual activity in the presence of 20 mM: 13% free papain, 38% immobilized papain
Ba2+
5 mM, 24% loss of activity (soluble enzyme), 9% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
Ca2+
-
residual activity in the presence of 20 mM: 10% free papain, 48% immobilized papain
Ca2+
5 mM, 22% loss of activity (soluble enzyme), 6% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
chagasin
-
-
-
chagasin
protease inhibitor, inhibits all C1 family proteases
-
E64
-
0.025 mg/ml, 65% inhibition
E64
-
strong irreversible inhibition in vivo
Mg2+
-
residual activity in the presence of 20 mM: 20% free papain, 57% immobilized papain
Mg2+
5 mM, 19% loss of activity (soluble enzyme), 4% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
Mn2+
-
residual activity in the presence of 20 mM: 0% free papain, 18% immobilized papain
Mn2+
5 mM, 44% loss of activity (soluble enzyme), 31% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
Zn2+
-
residual activity in the presence of 20 mM: 0% free papain, 16% immobilized papain
Zn2+
5 mM, 51% loss of activity (soluble enzyme), 45% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
additional information
loosely packed papain prosegment displays inhibitory activity but can also function as activator for the mature enzyme, overview
-
additional information
-
no inhibition by synthetic cyclic peptide CTSPRLHPCGGGS-NH2, interaction anaylsis of enzyme with diverse synthetic peptides in a phage display assay, overview
-
additional information
-
dipeptide vinyl sultams, synthesized via the Wittig-Horner reaction, show poor or no inhibition of papain in contrast to falcipain-2 of Plasmodium falciparum, interaction analysis, overview
-
additional information
-
several buffers decrease the activity of the n-propanol dehydrated, immobilized enzyme in low-water tert-butanol medium, overview
-
additional information
-
not inhibited by barley cystatin protease inhibitor-4 (Q86P), barley cystatin protease inhibitor-4 (N-term-DELTAA142 (Q86P)), barley cystatin protease inhibitor-4 (N-term-DELTAL150 (Q86P)), barley cystatin protease inhibitor-4 (DELTAT143-C-term), barley cystatin protease inhibitor-4 (DELTAT143-C-term (N177K)), barley cystatin protease inhibitor-4 (DELTAG151-C-term), and barley cystatin protease inhibitor-4 (DELTAG151-C-term (N177K))
-
additional information
immobilization of papain by covalent attachment on Sepharose 6B activated by using cyanogen bromide brings about resistance against the inhibitory effects of various bivalent metal ions with respect to papain
-
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0.048
alpha-benzoyl-L-argininamide
-
with Cys as activator
0.77
benzoyl-thiocarbamic acid
-
-
16
benzoyl-thiocarbamic acid ethyl ester
-
-
0.3
benzoyl-thiocarbamic acid methyl ester
-
-
0.221 - 0.616
benzyl-Phe-Val-Arg-4-nitroanilide
0.94 - 5.6
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide
1.296 - 2.03
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide
1.8
benzyloxycarbonyl-L-citrullyl-L-Arg 4-methylcoumarin-7-amide
-
mutant enzyme D158N
0.4 - 0.42
benzyloxycarbonyl-L-Phe-L-Arg 4-methylcoumarin-7-amide
0.089 - 1.48
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
0.06
carboxybenzoyl-Phe-Arg-7-(4-methyl)coumarylamide
100 mM sodium phosphate buffer, pH 6.0, containing 1 mM dithiothreitol and 1 mM EDTA
0.00385 - 1.765
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
0.119 - 0.2
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
0.027 - 0.1015
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
0.00691
N,N-diBoc-dityrosine-(isoniazid)2
-
pH 6.2, 25°C
6.63
N-(beta-phenylpropionyl)Gly methyl ester
-
-
0.11
N-(beta-phenylpropionyl)Gly methyl thiono ester
-
-
0.00212
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
-
pH 6.5, 27°C, Vmax: 2.14 miroM/sec
21.8
N-benzoyl-Gly methyl ester
-
-
0.301
N-benzoyl-Gly methyl thiono ester
-
-
21
N-benzoylglycinamide
-
38°C
0.008
N-benzyloxycarbonyl-Gly p-nitrophenyl ester
-
-
320
N-benzyloxycarbonyl-Gly-Gly
-
-
18.54
Nalpha-benzoyl-Gly methyl ester
-
-
0.0519 - 23
Nalpha-benzoyl-L-Arg ethyl ester
32 - 40
Nalpha-benzoyl-L-argininamide
10
Nalpha-benzoyl-L-citrulline methyl ester
-
-
20
Nalpha-benzyloxycarbonyl-L-histidinamide
-
-
0.73 - 1.84
ubiquitin-7-amido-4-trifluoromethylcoumarin
-
additional information
casein
0.221
benzyl-Phe-Val-Arg-4-nitroanilide
-
tartaric buffer containing 12% ethanol, pH 3.2, 25°C, papain from papaya latex
0.28
benzyl-Phe-Val-Arg-4-nitroanilide
-
McIlvaine buffer, pH 3.2, 25°C, papain from papaya latex
0.285
benzyl-Phe-Val-Arg-4-nitroanilide
-
McIlvaine buffer, pH 3.2, 25°C, papain from ripe fruit
0.344
benzyl-Phe-Val-Arg-4-nitroanilide
-
McIlvaine buffer + 12% ethanol, pH 3.2, 25°C, papain from papaya latex
0.464
benzyl-Phe-Val-Arg-4-nitroanilide
-
tartaric buffer containing 12% ethanol, pH 3.2, 25°C, papain from ripe fruit
0.616
benzyl-Phe-Val-Arg-4-nitroanilide
-
McIlvaine buffer + 12% ethanol, pH 3.2, 25°C, papain from ripe fruit
0.94
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/S205E
2.27
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide
-
-
5.6
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/V157G/S205E
1.296
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/S205E
2.03
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/V157G/S205E
0.4
benzyloxycarbonyl-L-Phe-L-Arg 4-methylcoumarin-7-amide
-
recombinant wild-type enzyme
0.42
benzyloxycarbonyl-L-Phe-L-Arg 4-methylcoumarin-7-amide
-
commercial enzyme preparation
0.089
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
-
-
0.191
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/S205E
0.43
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/V157G/S205E
1.48
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
-
-
0.0000082
casein
-
native enzyme
0.00057
casein
-
papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22°C
0.00061
casein
-
pH 9, 20°C, free papain
0.00062
casein
-
free papain, pH 7.5, 22°C
0.00062
casein
soluble enzyme, pH 7.5, 23°C
0.00066
casein
-
pH 9, 20°C, immobilized papain
0.00079
casein
-
papain immobilized on sepharose 6B, pH 7.5, 22°C
0.00079
casein
enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide, pH 7.5, 23°C
0.0063
casein
soluble enzyme, pH 7.5, 23°C
0.0065
casein
enzyme immobilized on multi-walled carbon nanotubes, pH 7.5, 23°C
530.7
casein
cotton-immobilized papain modified by pyromellitic anhydride, pH 8.0, 45°C
700.5
casein
cotton-immobilized papain modified by 1,2,4-benzenetricarboxylic anhydride, pH 8.0, 45°C
812.1
casein
cotton-immobilized unmodified papain, pH 8.0, 45°C
0.00385
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 1% methanol
0.005
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C
0.01243
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 5% methanol
0.02075
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 0.6% dimethylformamide
1.765
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 5% dimethylformamide
0.119
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
pH 6.2
0.119
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
at pH 6.2, in 10 mM sodium acetate, 0.1 mM EDTA and 1 mM cysteine
0.2
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
pH 7.4
0.2
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline
0.027
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
pH 6.2
0.027
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
at pH 6.2, in 10 mM sodium acetate, 0.1 mM EDTA and 1 mM cysteine
0.1015
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
pH 7.4
0.1015
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline
0.0519
Nalpha-benzoyl-L-Arg ethyl ester
-
-
0.0681
Nalpha-benzoyl-L-Arg ethyl ester
-
-
15
Nalpha-benzoyl-L-Arg ethyl ester
-
-
18
Nalpha-benzoyl-L-Arg ethyl ester
-
-
18
Nalpha-benzoyl-L-Arg ethyl ester
-
at 37°C
18.2
Nalpha-benzoyl-L-Arg ethyl ester
-
-
23
Nalpha-benzoyl-L-Arg ethyl ester
-
at 25°C
32
Nalpha-benzoyl-L-argininamide
-
25°C
40
Nalpha-benzoyl-L-argininamide
-
38°C
0.73
ubiquitin-7-amido-4-trifluoromethylcoumarin
-
pH not specified in the publication, 30°C, PLpro(1541-1858, DNA fragment)
-
1.84
ubiquitin-7-amido-4-trifluoromethylcoumarin
-
pH not specified in the publication, 30°C, PLpro(1600-1858, DNA fragment)
-
additional information
casein
0.245 g/ml (soluble enzyme), 0.252 g/ml (papain immobilized on hybrid nanoflowers), pH 7.4, 37°C
additional information
casein
the Km value of the papain immobilized on multi-walled carbon nanotubes experiences a slight increase, which suggests that the multi-walled carbon nanotubes do not significantly hinder the access of papain to substrate or release of product
additional information
additional information
-
-
-
additional information
additional information
-
KM value for human IgG with the immobilized enzyme is 0.55 mg/ml, the Km-value for the free enzyme is 1.08 mg/ml
-
additional information
additional information
-
kinetics and thermodynamics of soluble and immobilized enzyme at pH 7.0 and 40°C, overview
-
additional information
additional information
-
kinetics, stopped-flow method using interaction of the enzyme with seven different 2-pyridyl disulfide reactivity probes, overview
-
additional information
additional information
thermodynamics of the thermal unfolding of the recombinant prosegment, overview, pH-jump kinetics of the prosegment, overview
-
additional information
additional information
-
Km (casein) for immobilized papain is lower than for free papain
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3340
benzoyl-thiocarbamic acid
-
-
3.4
benzoyl-thiocarbamic acid ethyl ester
-
-
0.064
benzoyl-thiocarbamic acid methyl ester
-
-
180 - 309
benzyl-Phe-Val-Arg-4-nitroanilide
0.79 - 9.3
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide
0.42 - 8.14
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide
51 - 52
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
2.78 - 41.6
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
0.03 - 6.86
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
475 - 1773
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
243 - 1503
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
35.6
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
-
pH 6.5, 27°C
3.48
N-benzoyl-Gly methyl ester
-
-
16.4 - 28.5
Nalpha-benzoyl-L-Arg ethyl ester
0.79 - 0.96
ubiquitin-7-amido-4-trifluoromethylcoumarin
-
additional information
additional information
-
180
benzyl-Phe-Val-Arg-4-nitroanilide
-
McIlvaine buffer, pH 3.2, 25°C, papain from ripe fruit
189
benzyl-Phe-Val-Arg-4-nitroanilide
-
McIlvaine buffer, pH 3.2, 25°C, papain from papaya latex
215
benzyl-Phe-Val-Arg-4-nitroanilide
-
McIlvaine buffer + 12% ethanol, pH 3.2, 25°C, papain from papaya latex
217
benzyl-Phe-Val-Arg-4-nitroanilide
-
tartaric buffer containing 12% ethanol, pH 3.2, 25°C, papain from papaya latex
290
benzyl-Phe-Val-Arg-4-nitroanilide
-
McIlvaine buffer + 12% ethanol, pH 3.2, 25°C, papain from ripe fruit
309
benzyl-Phe-Val-Arg-4-nitroanilide
-
tartaric buffer containing 12% ethanol, pH 3.2, 25°C, papain from ripe fruit
0.79
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/V157G/S205E
1.18
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide
-
-
9.3
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/S205E
0.42
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/V157G/S205E
5.67
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/S205E
8.14
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/V157G/S205E
51
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
recombinant wild-type enzyme
52
benzyloxycarbonyl-L-Phe-L-Arg-7-amido-4-methylcoumarin
-
commercial enzyme preparation
2.78
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/V157G/S205E
16.9
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
-
mutant enzyme V133A/S205E
41.6
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide
-
-
0.00000028
casein
-
papain immobilized on sepharose 6B, pH 7.5, 22°C
0.00000035
casein
-
papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22°C
0.00000045
casein
-
free papain, pH 7.5, 22°C
0.0000038
casein
-
pH 9, 20°C, immobilized papain
0.0000046
casein
-
pH 9, 20°C, free papain
0.0102
casein
enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide, pH 7.5, 23°C
0.0162
casein
soluble enzyme, pH 7.5, 23°C
1.386
casein
cotton-immobilized papain modified by pyromellitic anhydride, pH 8.0, 45°C
1.5
casein
enzyme immobilized on multi-walled carbon nanotubes, pH 7.5, 23°C
1.604
casein
cotton-immobilized papain modified by 1,2,4-benzenetricarboxylic anhydride, pH 8.0, 45°C
1.7
casein
soluble enzyme, pH 7.5, 23°C
1.79
casein
cotton-immobilized unmodified papain, pH 8.0, 45°C
0.03 - 0.55
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 5% methanol
0.41
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 0.6% dimethylformamide
0.833
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C
2.77
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 1% methanol
3 - 6
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 1% methanol
6.86
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 5% methanol
475
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
at pH 6.2, in 10 mM sodium acetate, 0.1 mM EDTA and 1 mM cysteine
1773
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline
243
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
at pH 6.2, in 10 mM sodium acetate, 0.1 mM EDTA and 1 mM cysteine
1503
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline
16.4
Nalpha-benzoyl-L-Arg ethyl ester
-
-
24
Nalpha-benzoyl-L-Arg ethyl ester
-
-
28.5
Nalpha-benzoyl-L-Arg ethyl ester
-
-
0.79
ubiquitin-7-amido-4-trifluoromethylcoumarin
-
pH not specified in the publication, 30°C, PLpro(1541-1858, DNA fragment)
-
0.96
ubiquitin-7-amido-4-trifluoromethylcoumarin
-
pH not specified in the publication, 30°C, PLpro(1600-1858, DNA fragment)
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
kcat (casein) for immobilized papain is much lower than for free papain
-
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30
-
residual activity: 70% free papain, 40% immobilized papain
35.3
-
pH 2.0, first transition midpoint in absence of urea
4
-
residual activity after 30 storage: 0% free papain, 80% immobilized papain
44.2
-
pH 2.0, first transition midpoint in presence of 0.8 M urea
45
pH 3.2: inactivation constant: 0.0046/min
51
pH 3.2, Tm-value: 51.34°C
53.3
-
pH 2.0, second transition midpoint in absence of urea
56
-
at pH 2.0, partially reduced papain, single cooperative transition with a midpoint at 55.61°C
66.9
-
pH 2.0, second transition midpoint in presence of 0.8 M urea
85
-
10 min, in 2 mM EDTA solution with 0.08 M Cys, increase in activity
95
-
10 min, in 2 mM EDTA solution with 0.08 M Cys, about 80% loss of activity
22
-
room temperature, pH 8.7, 95% loss of activity after 8 days, then the preparation maintains constant activity over an 86-day period, papain included in porous glass
22
-
residual activity after 30 storage: 25% free papain, 80% immobilized papain
25
-
pH 7.0, 1 h, 49.8% loss of activity
25
pH 3.2, 30 min, 5% loss of activity
40
-
pH 7.0, 1 h, 24.9% loss of activity
40
-
single disulfide reduced carboxymethylated papain, at neutral pH, the protein started unfolding after 40°C
50
-
oxidized, inactive enzyme, in absence of activator, 67% of the initial activity remains after 28 days
50
pH 3.2: inactivation constant: 0.012/min
55
390 min, the soluble enzyme retains 41.9% of its activity, enzyme immobilized on hybrid nanoflowers retains 77.2% of its activity
55
pH 3.2: inactivation constant: 0.037/min
60
-
pH 7.0, 1 h, 33.6% loss of activity
60
-
half-life of wild-type, mutant K174R/V32S and mutant K174R/V32S/G36S is 77, 114, and 171 min, respectively
60
pH 3.2: inactivation constant: 0.1/min
65
-
pH 5.0, complete loss of activity after 7 days
65
-
half-life of wild-type, mutant K174R/V32S and mutant K174R/V32S/G36S is 35, 45, and 80 min, respectively
70
-
pH 7.0, 1 h, 53.9% loss of activity
70
-
single disulfide reduced carboxymethylated papain, at neutral pH, midpoint of transition is 70.33°C
70
-
30 min, the immobilized enzyme is completely stable, while the soluble enzyme loses activity
70
-
the native enzyme has a half-life of 6 h at 70°C
75
-
10 min, in 2 mM EDTA solution with 0.08 M Cys, increase in activity
75
-
2 h, free papain loses 60% of its activity, papain immobilized on the poly(glycidyl methacrylate-co-ethylene dimethylacrylate) monolith loses 10% of its activity
75
-
the native enzyme loses nearly 50% of its activity after heating at 75°C for 40 min, and it retains only 20% activity after heating for 80 min
75
-
free enzyme loses 75% of its activity after 300 min incubation at 75°C
75
-
immobilized enzyme loses 66% of its activity after 300 min incubation at 75°C
80
-
stable up to
80
-
pH 7.0, 1 h, 81.9% loss of activity
80
15% activity of immobilized pyromellitic papain after 4 h at pH 8.0
80
total activity losses for the cotton-immobilized unmodified papain and immobilized benzenetricarboxylic papain after 4 at pH 8.0
80
at 80°C, the enzyme immobilized on multi-walled carbon nanotubes retains more than 70% of the initial activity after 1 h incubation. A nearly complete inactivation of free papain is observed
80
half-life: 18 min (soluble enzyme). Immobilized papain retains 80% of its original activity after 1 h incubation
90
-
pH 7.0, 1 h, 95.3% loss of activity
90
-
half life after 60 storage: 5% free papain, 30% immobilized papain
90
-
residual activity: 30% free papain, 80% immobilized papain
90
half-life: 6 min (soluble enzyme), 40 min (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide). Immobilized papain retains 45% of its original activity after 1 h incubation
90
the enzyme immobilized on multi-walled carbon nanotubes retains above 50% of the initial activity after 1 h incubation while the activity of the free enzyme is completely inactivated after 1 h incubation
additional information
-
the enzyme is stable to heat in the oxidized, inactive form, activity is rapidly lost in presence of 2-mercaptopropionic acid, hippuric acid alters heat stability
additional information
-
temperature and guanidine hydrochloride induced unfolding transitions of papain at pH 2.0 are biphasic, implying independent and sequential unfolding of its two domains. The N-domain unfolds initially
additional information
-
thermal denaturation studies show that the binding of Ca2+ and Mg2+ brings about change in the thermal stability of papain at various concentrations of these metal ions. No significant change in the alpha-helix and beta-sheet structure of the papain upon binding of these metal ions
additional information
thermal unfolding of the prosegment, in acid medium the enzyme unfolds in a globule-like conformation, irreversible without intermediate states, overview
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food industry
combination of ultrasound and papain is more beneficial for improving functional properties of meat compared with the individual treatment
analysis
-
use of the enzyme in sequence determination
analysis
-
study on the cross-sectional distribution of methylene blue and papain in porous silicon layers by TOF-SIMS. The larger Papain molecule distributes itself in a similar manner to methylene blue demonstrating larger molecules can be effectively incorporated into such pore structures
analysis
-
study on the mixed micellar behavior of anionic surfactant, sodium dodecylsulfate, and cationic surfactant, dodecylethyldimethylammonium bromide, in aqueous solution of papain. The effect of concentration of papain on mixed micellar behavior indicates that with increase in the concentration of protein, the critical aggregation concentration and critical micellizationconcentration values increase. The unfolding of the polypeptide chain in the presence of mixed surfactant has been observed
biotechnology
-
immobilization of papain and dehydration by n-propanol in low-water media at pH 6.4 and 25°C in 150 mM sodium phosphate buffer, stability is increased by solid state cysteine, overview
biotechnology
-
papain immobilization on magnetic composite microspheres at pH 8.0 and 30°C, quantification and kinetics, overview, the immobilized enzyme exhibits better environmentally adaptability and reusability than the soluble enzyme
biotechnology
the enzyme plays a key role in biotechnology and has a range of important applications in cell isolation, leather, cosmetic, textiles, detergents, food, and pharmaceutical industries
biotechnology
-
evaluation of toxic and mutagenic potential of papain and its potential antioxidant activity against induced-H2O2 oxidative stress in Escherichia coli strains by cytotoxicity assay, growth inhibition test, WP2-mutoxitest and plasmid-DNA treatment, and agarose gel electrophoresis. Papain exhibits negative results for all tests
biotechnology
-
immobilisation of papain on gold nanorods enhances enzyme stability and efficiency, opening new opportunities for biotechnological applications
industry
papain has many uses and functions in a variety of industries: clarifying beer, meat tenderization, preservation of spices, contact lens cleaners, detergents, pet food palatability, digestive aids, blood stain remover, blood coagulant and cosmetics
industry
the cotton fabric immobilized modified papain has potential applicationsin the functional textiles field
industry
-
the enzyme with high biological activity and the decomposing ability is widely used in the lines of medical application, cell isolation, food, detergents, leather, textile, cosmetic and pharmaceutical industry
industry
catalytic properties of papain immobilized on hybrid nanoflowers are enhanced compared with that of free papain. The hybrid nanoflowers exhibit excellent reusability, high thermostability, long storage life and great potential in industrial applications
industry
immobilization on multi-walled carbon nanotubes is beneficial to the industrial applications because of its potential to be easily separated from the end product at the end of the reaction, reuse for multiple times and allow the development of multiple enzyme reaction system
industry
papain combined with chitosan-sodium alginate pretreated with the appropriate ultrasound can be effective technique for improving the activity of immobilized enzymes as a result of changes in its structure and intermolecular interactions. It is important to extend the application of chitosan-sodium alginate gel in the immobilized enzyme industry
medicine
-
used for wound debridement, the removal of necrotic tissue
medicine
-
used in external treatment of hard tissue, wart and scar tissue removal, acne treatment, depilation, skin cleansing treatment, inclusing in toothpaste. Papain is used in preparation of Tyr derivatives which are used for treatment of Parkinsonism and for the preparation of tetanus vaccines and immunoglobulin samples for intravenous injection
medicine
-
enzyme is used for a number of biomedical applications
medicine
papain is widely used for many medical and para-medical purposes such as to assist protein digestion in chronic dyspepsia, gastric fermentation, gastritis, removal of necrotic tissue, preparation of tyrosine derivatives for the treatment of Parkinsonism, preparation of tetanus vaccines, skin cleansing agents and acne treatment
medicine
-
effects of papain and neuraminidase enzyme treatment on electrohydrodynamics and IgG-mediated agglutination of type A red blood cells. Papain treatment results in a significant reduction of the hydrodynamic permeability of the external soft glycoprotein layer of the cells, reflecting a significant decrease in soft surface layer thickness and a loss in cell surface integrity/rigidity
medicine
-
entrapment of papain into a polymeric matrix in order to obtain a drug delivery system that can be used as medical device after sterilization by gamma radiation. Papain release and its activity in membranes containing 2% w/w papain in a silicone dispersion is not significantly affected by gamma irradiation
medicine
-
method for internalization of monoclonal antibodies based on papain digestion followed by flow cytometry. This method can identify whether the binding monoclonal antibody has internalized into the cell, with an additional advantage of accurately quantifying the internalized monoclonal antibody without altering cell morphology after papain digestion. The methodology can facilitate understanding of the efficiency of monoclonal antibody internalization and evaluation of the targeted killing capacity of the monoclonal antibody
medicine
-
study wether glucosamine modulates the immune and inflammatory responses to joint injury in organs proximal to glucosamine absorption using a papin-injected knee mouse model. Papain significantly degrades the proteoglycans in the injected knees by 2 days. Cartilage proteoglycan content is significantly higher in glucosamine-treated, papain-injected knees at Day 14. The peak concentration of serum pro-inflammatory cytokines occurrs earlier and decreases sooner in the injected, glucosamine-supplemented mice
medicine
a potential new self-emulsifying drug delivery system with mucolytic features for oral administration is developed. Using hydrophobic ion pairing, papain can be successfully included in the system. Within all formulations papain exhibits a mucolytic effect and accelerates a higher permeation in porcine intestinal mucus. Additionally a prolonged mucosal residence confirms that upon incorporation of enzyme, self-emulsifying drug delivery systems are awarded with the ability to overcome the intestinal barrier more easily. This system can be presented as a promising carrier capable to transport a therapeutic ingredient across the mucus barrier and finally improve its bioavailability
medicine
dental plaque is a causative factor for oral disease and a potential reservoir for respiratory infection in the elderly. Therefore, there is a critical need for the development of effective methods to remove oral biofilm. Proteases reduce oral biofilm in vivo in elderly subjects. Tablets containing actinidin remove tongue coating in elderly subjects. Oral Actinomyces biofilm is significantly reduced by the proteases papain, actinidin and trypsin. Papain and trypsin effectively digest the major fimbrial proteins, FimP and FimA, from Actinomyces. Actinidin, papain and trypsin reduce multispecies biofilm that is reconstructed in vitro. Papain and trypsin inhibit formation of multispecies biofilm in vitro
nutrition
-
papain is used in the preparation of fish protein concentrates from fish waste
nutrition
-
chill-proofing ability in beer
nutrition
-
used in the tenderisation of meat by its action on connective tissue and muscle protein. Beef is the only meat that is routinely subjected to papain tenderisation and the application of this technology is almost exclusively restricted to the USA
nutrition
-
the enzyme is used for the development of roast beef-like flavours by partial hydrolysis of proteins
nutrition
-
production of dehydrated pulses and beans
nutrition
-
papain is used in the brewing process for two main purposes: use in chillproofing and use in the mash tun to uncrease the yield of extract and therefore decrease malt consumption. The enzyme can be used in the production of specialized fish protein concentrate for use as a milk replacer when feeding calves and piglets. The enzyme is used to improve the protein dispersibility index of soya flour. Treatment of oil seed cake to incrase the nitrogen solubility index and/or the protein dispersibility index
nutrition
-
used extensively in food processing especially in tenderization of meat
synthesis
-
use as catalyst in asymetric synthesis of acyl derivatives and in peptide synthesis
synthesis
chemical modification of papain using different anhydrides of 1,2,4-benzenetricarboxylic and pyromellitic acids and immobilization on cotton fabric results in immobilized papain with optimum pH shifted from 6.0 to 9.0. Compared with immobilized native papain, the thermal stability and the resistance to alkali and washing detergent of immobilized modified enzyme are improved considerably. When the concentration of detergent is 20 mg/ml, the activity of the immobilized pyromellitic papain retains about 40% of its original activity, whereas the native papain is almost inhibited
synthesis
-
enzymatic hydrolysis of casein to produce free amino acids by papain in a two-phase system, which is composed of n-propanol, NaCl and water. In this system, the top phase contains more n-propanol and the bottom phase contains more NaCl and water. Papain and casein are mainly distributed in bottom phase, and free aromatic amino acids tyrosine, tryptophan and phenylalanine produced by enzymatic hydrolysis aere mainly in top phase. When the two-phase system consists of 44% n-propanol, 60 g/l NaCl, 0.15 g/l papain and 13 g/l casein at 55°C and pH 5.6, the transformation yield is 99.5%
synthesis
-
Fab antibody fragment production and purification by papain digestion of an intact monoclonal antibody. After digestion, separation of the Fab fragment from the Fc fragment and residual intact antibody is achieved using protein A affinity chromatography. The Fab fragments are of high quality suitable to produce diffraction quality crystals suitable for X-ray crystallographic analysis
synthesis
-
immobilization of papain on Sepharose 6B in the presence of different concentrations of cysteine affect the enzyme activity depending on cysteine concentration. The maximum specific activity is observed when papain was immobilized with 200 mM cysteine. The immobilization process results in significant enhancement of stability to temperature and extreme pH. After immobilization, the optimum temperature of papain activity increases by 20 degrees from 60 to 80°C and its optimum pH activity shifts from 6.5 to 8.0. Catalytic efficiency and specific activity of the immobilized enzyme do not significantly change after immobilization