Information on EC 3.4.22.2 - papain

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The expected taxonomic range for this enzyme is: Carica papaya

EC NUMBER
COMMENTARY
3.4.22.2
-
RECOMMENDED NAME
GeneOntology No.
papain
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'
show the reaction diagram
-
-
-
-
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'
show the reaction diagram
the His-Cys catalytic diad in free papain is fully protonated, -NH(+)/-SH. The experimental pKa of 8.62 for His159 imidazole in free papain is assigned to the -NH(+)/-SH and  -N/-SH equilibrium
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acyl transfer
-
-
hydrolysis
-
-
hydrolysis of peptide bond
-
-
hydrolysis of peptide bond
-
-
endopeptidase
-
polymerization
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Adolph's Meat Tenderizer
-
-
-
-
arbuz
-
-
-
-
EC 3.4.4.10
-
-
formerly
-
enzeco papain
-
-
-
-
papaine
-
-
-
-
papaya peptidase I
-
-
-
-
papaya proteinase 1
P00784
-
papayotin
-
-
-
-
PPI
-
-
-
-
PPI
P00784
-
summetrin
-
-
-
-
velardon
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-73-4
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(RS)-mandelic hydrazide + benzyloxycarbonyl-Ala
N1-(benzyloxycarbonyl-Ala)-N2-[(R)-mandelyl]hydrazine + N1-(benzyloxycarbonyl-Ala)-N2-[(S)-mandelyl]hydrazine
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
?
(RS)-mandelic hydrazide + hippuric acid
?
show the reaction diagram
-
-
-
-
?
(RS)-mandelic hydrazide + N(tert-amyloxycarbonyl)-Gly
(+)-N1-(tert-amyloxycarbonyl-Gly)-NH2-[(R)-mandelyl]hydrazine + (+)-N1-(tert-anhydroxycarbonyl-Gly)-N2-[(S)-mandelyl] hydrazine
show the reaction diagram
-
-
-
?
(RS)-mandelic hydrazide + N-(tert-butyloxycarbonyl)-Gly
(+)-N1-(tert-butyloxycarbonyl-Gly)-N2[(R)-mandelyl]hydrazine + (+)-(N1)-(tert-butyloxycarbonyl-Gly)-N2[(S)-mandelyl]hydrazine
show the reaction diagram
-
-
-
-
?
2-(amino)ethyl 2'-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
3-(amino)trimethylene 2'-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene) + H2O
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly + Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
show the reaction diagram
-
-
-
?
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene) + H2O
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly + Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
show the reaction diagram
-
-
-
?
4-(amino)-tetramethylene 2'-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
acetyl-Ala-Ala-Ala-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
acetyl-L-Phe-Gly-4-nitroanilide + H2O
acetyl-L-Phe-Gly + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
alpha-N-benzoyl-DL-Arg-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
azopeptide + peptides
show the reaction diagram
-
-
-
-
?
benzaldehyde + acetylacetone
3-benzylidenepentane-2,4-dione
show the reaction diagram
-
35% yield after 72 h at 25C or 55% yield after 81 h at 60C. 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
?
show the reaction diagram
-
pH 6.3, 20C
-
-
?
benzoyl-L-Arg-2-naphthylamide + H2O
benzoyl-L-Arg + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
benzoyl-thiocarbamic acid + H2O
N-benzoyl-Gly + SH2
show the reaction diagram
-
-
-
-
?
benzoyl-thiocarbamic acid ethyl ester + H2O
N-benzoyl-Gly + ethanethiol
show the reaction diagram
-
-
-
-
?
benzoyl-thiocarbamic acid methyl ester + H2O
N-benzoyl thioglycine + methanol
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ala methyl ester + L-Arg
benzyloxycarbonyl-Ala-Arg-OH
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-Arg-NH2 + Arg-NH2
benzyloxycarbonyl-Ala-Arg-Arg-NH2
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Ala-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Ala-4-aminoantipyrine + methanol
show the reaction diagram
P00784
-
-
-
?
benzyloxycarbonyl-Arg-Arg 4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-citrullyl-Arg 4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Gly-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Gly-4-aminoantipyrine + methanol
show the reaction diagram
P00784
-
-
-
?
benzyloxycarbonyl-Phe-Arg 4-methylcoumarin-7-amide + H2O
?
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu-4-nitroanilide + H2O
benzyloxycarbonyl-Phe-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
benzyloxycarbonyl-Ser-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Ser-4-aminoantipyrine + methanol
show the reaction diagram
P00784
-
-
-
?
beta-Ala-guanidinophenyl + L-Phe-NH2
beta-Ala-L-Phe-NH2 + beta-Ala + guanidinophenol
show the reaction diagram
-
-
31.6% yield of beta-Ala-LPhe-NH2
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
carboxybenzoyl-Phe-Arg-7-(4-methyl)coumarylamide + H2O
carboxybenzoyl-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
fluorogenic substrate
-
-
?
casein + H2O
L-tyrosine + ?
show the reaction diagram
-
-
-
-
?
CH3-CH2-2-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
CH3CO-(D-Phe)-NH-[CH2]2-2-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
CH3CO-(D-Phe)-O-[CH2]2-2-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
CH3CO-(L-Phe)-NH-[CH2]2-2-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
CH3CO-(L-Phe)-O-[CH2]2-2-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
CH3CO-NH-[CH2]2-2-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
CH3CO-O-[CH2]2-2-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
chitosan + H2O
low-molecular mass chitosan + chito-oligomeric-monomeric mixture
show the reaction diagram
-
depolymerization
product analysis by FTIR and NMR spectroscopy, overview
-
?
chitosan + H2O
low-molecular mass chitosan + chito-oligomeric-monomeric mixture
show the reaction diagram
-
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
-
-
?
CopA + H2O
?
show the reaction diagram
-
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
-
-
?
D-Ala -guanidinophenyl + L-Phe-NH2
D-Ala-L-Phe-NH2 + D-Ala + guanidinophenol
show the reaction diagram
-
-
11.6% yield of D-Ala-LPhe-NH2
-
?
DL-4-hydroxyphenylglycine methyl ester + H2O
?
show the reaction diagram
-
asymmetric hydrolysis
-
-
?
fibroin + H2O
?
show the reaction diagram
-
-
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
-
?
Glucagon + H2O
?
show the reaction diagram
-
-
-
-
?
Gly-guanidinophenyl
Gly + guanidinophenol
show the reaction diagram
-
-
94.8% yield for Gly
-
?
Gly-guanidinophenyl + D-Phe-NH2
Gly-D-Phe-NH2 + Gly + guanidinophenol
show the reaction diagram
-
-
22.9% yield for Gly-D-Phe-NH2 and 74.3% yield for Gly
-
?
Gly-guanidinophenyl + L-Ala-4-nitroanilide
Gly-L-Ala-4-nitroanilide + Gly + guanidinophenol
show the reaction diagram
-
-
96% yield for Gly-L-Ala-4-nitroanilide
-
?
Gly-guanidinophenyl + L-Ala-NH2
Gly-L-Ala-NH2 + Gly-OH + guanidinophenol
show the reaction diagram
-
-
87% yield for Gly-L-Ala-NH2 and 7.7% yield for Gly-OH
-
?
Gly-guanidinophenyl + L-Phe-NH2
Gly-L-Phe-NH2 + Gly + guanidinophenol
show the reaction diagram
-
-
92% yield of Gly-LPhe-NH2
-
?
Gly-guanidinophenyl + L-Phe-OtBu
Gly-L-Phe-OtBu + guanidinophenol
show the reaction diagram
-
-
11.8% yield for Gly-L-Phe-OtBu
-
?
Gly-guanidinophenyl + L-Pro-4-nitroanilide
Gly-L-Pro-4-nitroanilide + Gly + guanidinophenol
show the reaction diagram
-
-
90.3% yield for Gly
-
?
Gly-guanidinophenyl + L-Ser-4-nitroanilide
Gly-L-Ser-4-nitroanilide + Gly + guanidinophenol
show the reaction diagram
-
-
94% yield for Gly-L-Ser-4-nitroanilide
-
?
Gly-guanidinophenyl + L-Tyr-4-nitroanilide
Gly-L-Tyr-4-nitroanilide + Gly + guanidinophenol
show the reaction diagram
-
-
90.6% yield for Gly-L-Tyr-4-nitroanilide and 4.3% yield for Gly
-
?
Gly-guanidinophenyl + L-Tyr-NH2
Gly-L-Tyr-NH2 + Gly + guanidinophenol
show the reaction diagram
-
-
91.3% yield for Gly-L-Tyr-NH2 and 2.5% yield for Gly
-
?
Hemoglobin + H2O
?
show the reaction diagram
-
alpha-chain and beta-chain
-
-
?
hippuric acid + aniline
hippuryl anilide
show the reaction diagram
-
weak activity, 0.1% of the hydrolytic activity with N-benzoyl-L-argininamide
-
r
human IgG + H2O
fragment Fab + fragment Fc
show the reaction diagram
-
-
-
?
immunoglobulin M + H2O
IgMI +
show the reaction diagram
-
release of a basic subunit-like fragment which is designated IgMI, by proteolysis of the m-chain near the carboxyl terminus
-
?
L-Ala-guanidinophenyl + L-Phe-NH2
L-Ala-L-Phe-NH2 + L-Ala + guanidinophenol
show the reaction diagram
-
-
77.5% yield of L-Ala-LPhe-NH2
-
?
L-Arg-7-amido-4-methylcoumarin + H2O
L-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
L-Arg-guanidinophenyl + L-Phe-NH2
L-Arg-L-Phe-NH2 + L-Arg + guanidinophenol
show the reaction diagram
-
-
45.9% yield of L-Arg-LPhe-NH2
-
?
L-Asn-guanidinophenyl + L-Phe-NH2
L-Asn-L-Phe-NH2 + L-Asn + guanidinophenol
show the reaction diagram
-
-
6.1% yield of L-Asn-LPhe-NH2
-
?
L-Glu-guanidinophenyl + L-Phe-NH
L-Glu-L-Phe-NH2 + L-Glu + guanidinophenol
show the reaction diagram
-
-
68.5% yield of L-Glu-LPhe-NH2
-
?
L-glutamic acid diethyl ester + L-glutamic acid diethyl ester
L-Glu-gamma-diethyl ester polymer
show the reaction diagram
-
polymerization reaction
-
-
?
L-glutamic acid diethyl ester + L-glutamic acid diethyl ester
oligo-gamma-ethyl-L-glutamate
show the reaction diagram
-
oligomerization reaction
-
-
?
L-glutamic acid diethyl ester + N-alpha-benzoyl-L-arginine ethyl ester
N-alpha-benzoyl-L-arginine + N-alpha-benzoyl-L-argininyl-Glu-diethyl ester
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
L-glutamic acid triethyl ester shows higher affinity for papain than L-glutamic acid diethyl ester
-
-
?
L-Ile-guanidinophenyl + L-Phe-NH2
L-Ile-L-Phe-NH2 + L-Ile + guanidinophenol
show the reaction diagram
-
-
24.5% yield of L-Ile-LPhe-NH2
-
?
L-phenylalanine amide + H2O
L-phenylalanine + NH3
show the reaction diagram
-
-
-
-
?
L-Pro-L-Phe-L-Leu-4-nitroanilide + H2O
L-Pro-L-Phe-L-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Pro-Phe-Leu-4-nitroanilide + H2O
L-Pro-Phe-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
L-Thr-guanidinophenyl + L-Phe-NH2
L-Thr-L-Phe-NH2 + L-Thr + guanidinophenol
show the reaction diagram
-
-
90.7% yield of L-Thr-LPhe-NH2
-
?
lambda repressor + H2O
?
show the reaction diagram
-
no cleavage of the operator-bound repressor dimer
-
?
low molecular weight heparin + H2O
?
show the reaction diagram
-
-
-
-
?
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2 + H2O
?
show the reaction diagram
-
pH 6.2 or pH 7.4, 10 min, 37C
-
-
?
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
show the reaction diagram
-
FRET 2, fluorescence resonance energy transfer peptide 2
-
-
?
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N5-(5-carboxyfluorescein))-NH2 + H2O
?
show the reaction diagram
-
pH 6.2 or pH 7.4, 10 min, 37C
-
-
?
N(beta-phenylpropionyl)Gly methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-Trp p-nitrophenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-acetyl-L-tyrosinamide + H2O
N-acetyl-L-Tyr + NH3
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-DL-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-DL-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-alpha-benzoyl-L-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-L-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
N-benzoyl-Arg-p-nitroanilide + H2O
Nalpha-benzoyl-Arg + p-nitroanilide
show the reaction diagram
-
-
-
?
N-benzoyl-DL-arginine-2-naphthylamide + H2O
N-benzoyl-DL-arginine + 2-naphthylamine
show the reaction diagram
-
-
-
-
?
N-benzoyl-Gly ethyl ester + H2O
N-benzoyl-Gly + ethanol
show the reaction diagram
-
-
-
-
?
N-benzoyl-Gly methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzoyl-Gly methyl ester + H2O
N-benzoyl-Gly + methanol
show the reaction diagram
-
-
-
-
?
N-benzoylglycinamide + H2O
Nalpha-benzoyl-Gly + NH3
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Ala methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly 2-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + 2-nitrophenol
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly 3-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + 3-nitrophenol
show the reaction diagram
-
-
-
-
?
N-Benzyloxycarbonyl-Gly 4-nitrophenyl ester + H2O
N-Benzyloxycarbonyl-Gly + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly phenyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly-Gly + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-Gly-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
N-benzyloxycarbonyl-L-Glu diamide + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-glycine + H2O
?
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-histidinamide + H2O
Nalpha-benzoyl-L-His + NH3
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-leucinamide + H2O
Nalpha-benzoyl-L-Leu + NH3
show the reaction diagram
-
-
-
-
?
N-benzyloxycarbonyl-L-Lys + H2O
?
show the reaction diagram
-
-
-
-
?
n-propyl 2-pyridyl disulfide + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-Arg-p-nitroanilide + H2O
Nalpha-benzoyl-Arg + p-nitroaniline
show the reaction diagram
-
-
-
?
Nalpha-benzoyl-DL-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-DL-Arg + 4-nitroaniline
show the reaction diagram
P00784
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-Arg ethyl ester
?
show the reaction diagram
-
-
-
-
-
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-argininamide + H2O
Nalpha-benzoyl-L-Arg + NH3
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-arginine ethyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-citrulline methyl ester + H2O
?
show the reaction diagram
-
-
-
-
?
Nalpha-benzoyl-L-lysinamide + H2O
Nalpha-benzoyl-L-Lys + NH3
show the reaction diagram
-
-
-
-
?
ovalbumin + H2O
?
show the reaction diagram
-
-
-
-
?
oxidized beta-chain of insulin + H2O
?
show the reaction diagram
-
-
-
-
?
Phe-Arg-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
?
phthalyl-Phe-Leu-p-nitroanilide + H2O
phthalyl-Phe-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
?
sarcoendoplasmic reticulum Ca2+-ATPase 1 + H2O
?
show the reaction diagram
-
-
-
-
?
succinyl-Phe-Leu-4-methylcoumaryl-7-amide + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Phe-Leu-4-nitroanilide + H2O
succinyl-Phe-Leu + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
succinyl-Phe-Leu-p-nitroanilide + H2O
?
show the reaction diagram
-
-
-
?
succinyl-Phe-Leu-p-nitrophenol + H2O
?
show the reaction diagram
-
-
-
?
tarocystatin + H2O
?
show the reaction diagram
-
the C-terminal cystatin-like extension of tarocystatin is easily digested by papain
-
-
?
Z-Phe-Arg-4-nitroanilide + H2O
Z-Phe-Arg + 4-nitroaniline
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
FRET 1, fluorescence resonance energy transfer peptide 1
-
-
?
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
?
-
P00784
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
casein + H2O
?
show the reaction diagram
-
-
-
-
?
tarocystatin + H2O
?
show the reaction diagram
-
the C-terminal cystatin-like extension of tarocystatin is easily digested by papain
-
-
?
chitosan + H2O
low-molecular mass chitosan + chito-oligomeric-monomeric mixture
show the reaction diagram
-
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
-
-
?
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
?
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
1 mM, enzymatic activity increases to a maximum of 18%
Mg2+
-
1 mM, enzymatic activity increases to a maximum of 24%
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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
1,3-Dibromoacetone
-
-
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
ascorbic acid
-
strong
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
Bromoacetic acid
-
-
carbobenzyloxy-leucinyl-leucinyl-leucinal
-
-
-
chagasin
-
-
-
chagasin
-
protease inhibitor, inhibits all C1 family proteases
-
Chloroacetate
-
-
CNWAAGYNCGGGS-NH2
-
synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
CNWTLGGYKCGGGS-NH2
-
synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
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
-
CWEWGGWHCGGSS-OH
-
synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
CWSMMGFQCGGGS-NH2
-
weak inhibition, synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
Cystatin
-
-
-
cystatin B
-
-
-
cystatin SN
-
-
-
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
E64
-
0.025 mg/ml, 65% inhibition
E64
-
strong irreversible inhibition in vivo
endopin 2
-
highly effective inhibition, cross-class inhibition of papain and elastase. Localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells
-
ethyl-(RS)-2-(2-oxo-4-phenylazetidin-1-yl)acetate
-
weak inhibitor, irreversible
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
inhibitor of cysteine protease
-
-
-
iodoacetamide
-
-
iodoacetic acid
-
-
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
-
-
Leupeptin
-
-
methanol
-
number of papain active sites decreases with increase of inhibitor concentration
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
-
-
-
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
staccopin P1
-
-
-
staccopin P2
-
-
-
strepin P-1
-
-
-
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
-
methyl methanethiosulfonate
-
-
additional information
P00784
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))
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptopropionic acid
-
required, complete activation at 0.05 N when the enzyme concentration is 0.49 mM
cysteine
-
the requirement for reducing conditions during the activation process is investigated with 20 mM DTT or 20 mM cysteine, propapain does not convert to papain even after prolonged incubation with DTT, whereas in presence of 20 mM cysteine, the activation occurs between 30 and 40 min at 50C
EDTA
-
required for maximal activity
Reducing agents
-
e.g. 2,3-dimercaptopropanol, activates
-
Sodium borohydride
-
activates
thiol compounds
-
activate
glutathione
-
-
additional information
P00784
loosely packed papain prosegment displays inhibitory activity but can also function as activator for the mature enzyme, overview
-
additional information
-
alkylation of a cysteine residue in papain with a pyridoxamine results in a semi-synthetic enzyme papain-PX that has no detectable protease activity but has the ability to catalyze enantioselective reductive amination of alpha-keto acids such as alpha-ketoglutarate and pyruvate. Papain-PX reductively aminates the alkyl side chain of functionalized alpha-keto acids to give the respective alpha-amino acids with enantioselectivities greater than 70%
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00385
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 1% methanol
0.005
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C
0.01243
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 5% methanol
0.02075
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 0.6% dimethylformamide
1.765
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 5% dimethylformamide
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
-
-
0.94
-
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
1.8
-
benzyloxycarbonyl-L-citrullyl-L-Arg 4-methylcoumarin-7-amide
-
mutant enzyme D158N
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
-
-
0.06
-
carboxybenzoyl-Phe-Arg-7-(4-methyl)coumarylamide
-
100 mM sodium phosphate buffer, pH 6.0, containing 1 mM dithiothreitol and 1 mM EDTA
0.0000082
-
casein
-
native enzyme
0.00057
-
casein
-
papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22C
0.00062
-
casein
-
free papain, pH 7.5, 22C
0.00079
-
casein
-
papain immobilized on sepharose 6B, pH 7.5, 22C
530.7
-
casein
-
cotton-immobilized papain modified by pyromellitic anhydride, pH 8.0, 45C
700.5
-
casein
-
cotton-immobilized papain modified by 1,2,4-benzenetricarboxylic anhydride, pH 8.0, 45C
812.1
-
casein
-
cotton-immobilized unmodified papain, pH 8.0, 45C
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; pH 6.2
0.2
-
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline; pH 7.4
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; pH 6.2
6.63
-
N-(beta-phenylpropionyl)Gly methyl ester
-
-
0.11
-
N-(beta-phenylpropionyl)Gly methyl thiono ester
-
-
-
21.8
-
N-benzoyl-Gly methyl ester
-
-
0.301
-
N-benzoyl-Gly methyl thiono ester
-
-
-
21
-
N-benzoylglycinamide
-
38C
0.008
-
N-benzyloxycarbonyl-Gly p-nitrophenyl ester
-
-
320
-
N-benzyloxycarbonyl-Gly-Gly
-
-
18.54
-
Nalpha-benzoyl-Gly methyl ester
-
-
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
-
at 37C
18
-
Nalpha-benzoyl-L-Arg ethyl ester
-
-
18.2
-
Nalpha-benzoyl-L-Arg ethyl ester
-
-
23
-
Nalpha-benzoyl-L-Arg ethyl ester
-
at 25C
32
-
Nalpha-benzoyl-L-argininamide
-
25C
40
-
Nalpha-benzoyl-L-argininamide
-
38C
10
-
Nalpha-benzoyl-L-citrulline methyl ester
-
-
20
-
Nalpha-benzyloxycarbonyl-L-histidinamide
-
-
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; pH 7.4
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
-
-
-
additional information
-
additional information
P00784
thermodynamics of the thermal unfolding of the recombinant prosegment, overview, pH-jump kinetics of the prosegment, 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
-
kinetics and thermodynamics of soluble and immobilized enzyme at pH 7.0 and 40C, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
0.55
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 5% methanol
0.41
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 0.6% dimethylformamide
0.833
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C
2.77
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 1% methanol
3
6
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 1% methanol
6.86
-
4(4'-dimethylaminophenylazo)benzoyl-Lys-Phe-Gly-Gly-Ala-Ala-(5-[(2-aminoethyl)amino]naphthalene)
-
pH 6.8, 40C, in presence of 5% methanol
3340
-
benzoyl-thiocarbamic acid
-
-
3.4
-
benzoyl-thiocarbamic acid ethyl ester
-
-
0.064
-
benzoyl-thiocarbamic acid methyl ester
-
-
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 4-methylcoumarin-7-amide
-
recombinant wild-type enzyme
52
-
benzyloxycarbonyl-L-Phe-L-Arg 4-methylcoumarin-7-amide
-
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, 22C
0.00000035
-
casein
-
papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22C
0.00000045
-
casein
-
free papain, pH 7.5, 22C
1.386
-
casein
-
cotton-immobilized papain modified by pyromellitic anhydride, pH 8.0, 45C
1.604
-
casein
-
cotton-immobilized papain modified by 1,2,4-benzenetricarboxylic anhydride, pH 8.0, 45C
1.79
-
casein
-
cotton-immobilized unmodified papain, pH 8.0, 45C
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
3.48
-
N-benzoyl-Gly methyl ester
-
-
16.4
-
Nalpha-benzoyl-L-Arg ethyl ester
-
-
24
-
Nalpha-benzoyl-L-Arg ethyl ester
-
-
28.5
-
Nalpha-benzoyl-L-Arg ethyl ester
-
-
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
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00035
-
casein
-
papain immobilized on sepharose 6B, pH 7.5, 22C
8333
0.00061
-
casein
-
papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22C
8333
0.00064
-
casein
-
free papain, pH 7.5, 22C
8333
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.096
-
acetyl-Phe-Gly-S-nitrosopenicillamine
-
pH 6.2, 25C
0.0000033
-
benzyloxycarbonyl-Phe-Ala-glyoxal
-
pH 7.03, 25C
0.000000036
-
chagasin
-
inactivation of papain is very fast, rate constant for inactivation is 1500 mM/s
-
0.0063
-
CNWAAGYNCGGGS-NH2
-
pH 6.8, 37C
0.0286
-
CNWTLGGYKCGGGS-NH2
-
pH 6.8, 37C
0.0000018
-
CpPRI
-
pH 7.5, 37C
-
0.0071
-
CWEWGGWHCGGSS-OH
-
pH 6.8, 37C
0.00000001
-
cystatin SN, cystatin SN variant G12A/G13A, cystatin SN variant P106G/W107G
-
below
-
0.000057
-
cystatin variant Y56G/T57G/V58G
-
-
-
0.0000019
-
papain prosegment
P00784
recombinant prosegment, pH 7.0, 20C, inhibition kinetics
-
0.356
-
S-nitroso-N-acetyl-DL-penicillamine
-
pH 6.2, 25C
0.449
-
S-nitrosocaptopril
-
pH 6.2, 25C
0.305
-
S-nitrosoglutathione
-
pH 6.2, 25C
0.618
-
D-glucose-2S-nitroso-N-acetyl-penicillamine
-
pH 6.2, 25C
additional information
-
additional information
-
inhibition constants for various barley cystatin protease inhibitor variants
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.7
-
(eta5-C5H5)Fe(CO)3 eta1-N-succinimidato
-
pH 6.5, temperature not specified in the publication
-
0.28
-
(eta5-C5H5)Mo(CO)3 eta1-N-succinimidato
-
pH 6.5, temperature not specified in the publication
-
0.48
-
(eta5-C5H5)W(CO)3 eta1-N-succinimidato
-
pH 6.5, temperature not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.059
-
-
activity of immobilized papain dehydrated by n-propanol in low-water tert-butanol media
1.65
-
-
purified enzyme at pH 10.5 and 60C
1.78
-
-
purified enzyme, substrate chitosan
121
-
-
mutant K174R/V32S, pH 6.5, 37C
125.9
-
-
recombinant papain, in 100 mM sodium acetate and 2 mM EDTA at pH 6.5
128
-
-
wild-type, pH 6.5, 37C
130
-
-
mutant K174R/V32S/G36S, pH 6.5, 37C
221.7
-
-
commercial papain, in 100 mM sodium acetate and 2 mM EDTA at pH 6.5
additional information
-
-
growth inhibition of Bacillus cereus strain F4810 and Escherichia coli strain D21 via the chitosanolytic activity of the enzyme
additional information
-
-
toxic effects on insect larvae by latex enzyme and protease activity in papaya leaves, overview
additional information
-
-
1,2,4-benzenetricarboxylic papain has 97.73% relative activity compared to the unmodified enzyme; pyromellitic papain has 95.88% relative activity compared to the unmodified enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.5
-
-
depolymerization of chitosan
6
6.5
-
-
6
-
-
about
6
-
-
enzyme immobilized on cotton fabric; maximum activity of native papain activity
6
-
-
assay at
6.3
-
-
20C
6.4
-
-
assay at
6.5
-
-
soluble enzyme
6.5
-
-
free enzyme
6.5
-
-
hydrolysis of casein, soluble enzyme
6.6
-
P00784
assay at
6.8
-
-
assay at
7
-
-
assay at
7
-
-
hydrolysis of casein, immobilized enzyme
7.1
-
-
The effect of initial pH and temperature on adsorption capacity for papain on the chitosan-coated nylon composite membranes in Tris-HCl buffer is tested, an optimum point of maximum adsorption capacity obtained as 26.61 mg/g at 39C, pH 7.05 by fixing 8 mg/ml initial papain concentration. Adsorption capacity of papain increases from 26.61 to 27.85 mg/g when the papain concentration increases from 8 to 11 mg/ml.
7.2
-
-
hydrolysis of alpha-N-benzoyl-L-Arg ethyl ester, soluble enzyme
7.5
-
-
optimal storage stability for the soluble and immobilize enzyme at 5C
8
-
-
immobilized enzyme
8
-
-
enzyme immobilized on sepharose 6B in presence or absence of 200 mM cysteine
8.2
-
-
hydrolysis of alpha-N-benzoyl-L-Arg ethyl ester, immobilized enzyme
9
-
-
1,2,4-benzenetricarboxylic-modified and pyromellitic acid-modified enzyme immobilized on cotton fabric; enzyme modified by 1,2,4-benzenetricarboxylic anhydride or pyromellitic anhydride
9.5
-
-
hydrolysis of benzyloxycarbonyl-Ala methyl ester
additional information
-
P00784
pH-jump kinetics of the prosegment at pH 8 to 3.4
additional information
-
-
processing of propapain to mature papain is triggered by low pH and is stimulated by high temperatures
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.8
4.5
-
conditions for in vitro activation of the refolded propapain to mature papain are determined, the highest rates of activation are observed between pH 3.8 and 4.5, while the rates are greatly reduce at pH higher than 6
4.1
8.5
-
-
5
10
-
pH profile of soluble and immobilized enzyme
5
8
-
pH 5.0: about 70% of maximal activity, pH 8.0: about 85% of maximal activity
6.2
7.4
-
10 min, 37C
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
P00784
assay at
20
-
-
pH 6.3
25
-
-
assay at
37
-
-
assay at
37
-
-
depolymerization of chitosan
37
-
-
assay at; pH 6.2 or pH 7.4, 10 min
40
-
-
assay at
40
-
-
-
50
-
-
wild-type
60
-
-
free enzyme
60
-
-
mutant K174R/V32S
60
-
-
Knoevenagel reaction
60
-
-
hydrolysis of casein, soluble and immobilized enzyme
65
-
-
soluble enzyme
65
-
-
mutant K174R/V32S/G36S
65
-
-
hydrolysis of alpha-N-benzoyl-L-Arg ethyl ester, soluble enzyme
75
-
-
hydrolysis of alpha-N-benzoyl-L-Arg ethyl ester, immobilized enzyme
80
-
-
immobilized enzyme
80
-
-
the activity of immobilized pyromellitic papain has a vital peak at 80C, which may be attributed largely to the particular enzyme structure; the enzyme activity of cotton-immobilized native and papain modified by 1,2,4-benzenetricarboxylic anhydride and pyromellitic anhydride increased gradually with temperature, and the maximum activity is obtained at 80C
80
-
-
enzyme immobilized on sepharose 6B in presence or absence of 200 mM cysteine
85
-
-
immobilized enzyme
additional information
-
-
temperature-dependences of the second-order rate constants of the reaction involving the catalytic site thiol, overview, stopped-flow method
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
90
-
temperature profile of soluble and immobilized enzyme
25
70
-
25C: about 65% of maximal activity, 70C: about 60% of maximal acticity
50
100
-
50C: about 35% of maximal activity, 100C: about 95% of maximal activity, immobilized enzyme
60
80
-
the activity of immobilized unmodified papain and immobilized benzenetricarboxylic papain are increased stably over a period of 60 to 80C without significant change
additional information
-
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.4
-
P00784
recombinnat prosegment, isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
green unripe fruit
Manually annotated by BRENDA team
-
maximal concentration is reached early in the development of the fruit
Manually annotated by BRENDA team
-
in leaves
Manually annotated by BRENDA team
-
estimated as a fraction of papaya latex
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20700
-
-
enzyme from commercial chymopapain, equilibrium measurement
23000
-
-
SDS-PAGE
23700
-
-
equilibrium sedimentation
23800
-
-
enzyme from spray-dried latex, equilibrium measurement
42000
-
-
propapain containing respective fusion-tag sequence, determined by SDS-PAGE
additional information
-
-
during processing of propapain to papain, 2 intermediates are observed in the range of 30-38 kDa at 20 min incubation at 50C indicating that processing of propapain to papain occurs in a stepwise manner
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 23429, calculation from amino acid sequence
?
-
x * 23406, calculation from amino acid sequence
additional information
-
secondary structure determination of unfolded enzyme and of partially unfolded intermediate in presence of denaturing 1,1,1,3,3,3-hexafluoroisopropanol and 2,2,2-trifluoroethanol at pH 2.0 or pH 7.0, determination by binding to fluorescent 1-anilino-8-sulfonic acid via tryptophan residues, overview
additional information
P00784
the papain prosegment shows a high degree of conformational flexibility, proenzyme structure molecular modeling
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
no modification
-
nonglycosylated enzyme
proteolytic modification
P00784
the proenzyme is activated by cleavage of the prosegment
side-chain modification
-
propapain is activated by intramolecular thiol-disulfide exchange which is catalyzed by cysteine
side-chain modification
-
the enzyme is produced as an inactive precursor
side-chain modification
-
propapain is a thio-containing but catalytically inactive protein, that is a structural isomer of papain that can be transformed into papain by thiol-disulfide interchange initiated by addition of a suitable nucleophile such as thiolate
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a complex of chagasin, a protein inhibitor from Trypanosoma cruzi, and papain is crystallized by using the hanging-drop vapor diffusion method at 18C, the high-resolution crystal structure shows an inhibitory wedge comprising three loops, which forms a number of contacts responsible for the high-affinity binding, the present chagasin-papain complex provides a reliable model of chagasin-cruzipain interactions
-
complex with benzyloxycarbonyl-Arg-Leu-Val-Gly-CHN2
-
complex with E-64; enzyme structure of the complex of papain with N-[N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl]-isoamylamide
-
crystal structure of the complex of papain with recombinant human stefin B
-
crystal structure of the papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide complex at 1.7 -A resolution
-
enzyme structure of the complex of papain with N-[N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl]-isoamylamide
-
enzyme structure of the complex of papain with N-[N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl]-isoamylamide; structure of papain complexed with benzyloxycarbonyl-L-Phe-L-Ala-L-Ala chloromethylketone
-
hanging drop vapour diffusion method with 50% ethanol, 0.01 M sodium acetate, crystallization of a papain-inhibitor of protease complex is not possible
-
papain complexed with cathepsin B-specific covalent-type inhibitor
-
papain-inhibitor complex with benzyloxycarbonyl-Leu-Leu-leucinal or benzyloxycarbonyl-L-Leu-L-Leu methoxymethyl ketone
-
papain-leupeptin complex
-
tarocystatin-papain complex and C-terminal cystatin-like extension-papain complex, hanging drop vapor diffusion method, the tarocystatin-papain complex is crystallized from a drop containing 15% PEG monomethyl ether 2000, 0.05 M sodium acetate trihydrate, pH 4.6, 0.1 M ammonium sulfate against a reservoir of 30% PEG monomethyl ether 2000, 0.1 M sodium acetate trihydrate, pH 4.6, and 0.2 M ammonium sulfate. The complex of CtE-papain is crystallized from a drop containing 0.05 M HEPES, pH 7.5, and 35% (v/v) 2-methyl-2,4-pentanediol against a reservoir of 0.1 M HEPES, pH 7.5, and 70% (v/v) 2-methyl-2,4-pentanediol
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
7
-
25C, stable at pH 7.0, acid unfolding at pH 2.0
2
-
-
the activity of papain is reduced to 35% at pH 2 and in the absence of detergents, at pH 2 papain exhibits a substantial amount of secondary structure and is relatively less denatured compared with 6 M guanidine hydrochloride but loses the persistent tertiary contacts of the native state
4
10
-
stable
4
-
-
rapid and irreversible inactivation, at elevated temperatures
6
11
-
the native enzyme rapidly decreases to the relative activity of 70%
7
10
-
the native papain displaying over 80% of its activity; the papain modified by by 1,2,4-benzenetricarboxylic anhydride and pyromellitic anhydride displaying over 80% of its activity
7
-
-
native papain loses its activity gradually above pH 7.0
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
25
-
-
pH 7.0, 1 h, 49.8% loss of activity
35.3
-
-
pH 2.0, first transition midpoint in absence of urea
40
-
-
single disulfide reduced carboxymethylated papain, at neutral pH, the protein started unfolding after 40C
40
-
-
pH 7.0, 1 h, 24.9% loss of activity
44.2
-
-
pH 2.0, first transition midpoint in presence of 0.8 M urea
50
-
-
oxidized, inactive enzyme, in absence of activator, 67% of the initial activity remains after 28 days
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 55.61C
60
-
-
half-life of wild-type, mutant K174R/V32S and mutant K174R/V32S/G36S is 77, 114, and 171 min, respectively
60
-
-
pH 7.0, 1 h, 33.6% loss of activity
65
-
-
half-life of wild-type, mutant K174R/V32S and mutant K174R/V32S/G36S is 35, 45, and 80 min, respectively
65
-
-
pH 5.0, complete loss of activity after 7 days
66.9
-
-
pH 2.0, second transition midpoint in presence of 0.8 M urea
70
-
-
single disulfide reduced carboxymethylated papain, at neutral pH, midpoint of transition is 70.33C
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 70C
70
-
-
pH 7.0, 1 h, 53.9% loss of 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 75C for 40 min, and it retains only 20% activity after heating for 80 min
75
-
-
10 min, in 2 mM EDTA solution with 0.08 M Cys, increase in activity
80
-
-
15% activity of immobilized pyromellitic papain after 4 h at pH 8.0; total activity losses for the cotton-immobilized unmodified papain and immobilized benzenetricarboxylic papain after 4 at pH 8.0
80
-
-
stable up to
80
-
-
pH 7.0, 1 h, 81.9% loss of activity
85
-
-
10 min, in 2 mM EDTA solution with 0.08 M Cys, increase in activity
90
-
-
pH 7.0, 1 h, 95.3% loss of activity
95
-
-
10 min, in 2 mM EDTA solution with 0.08 M Cys, about 80% loss of activity
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
-
-
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
-
P00784
thermal unfolding of the prosegment, in acid medium the enzyme unfolds in a globule-like conformation, irreversible without intermediate states, overview
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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
chemical modification using citraconic acid, phthalic acid, maleic acid, and succinic acid leads to an increased thermostability of the enzyme
-
free papain loses 60% of its activity after 2 h at 75C, papain immobilized on the poly(glycidyl methacrylate-co-ethylene dimethylacrylate) monolith loses 10% of its activity
-
Immobilization of papain after chemical modification increases its stability and reusability in alkaline conditions. After adding of detergent powder in distilled water (final concentration of 5-25 mg/ml) to the proteolytic activity test at 45C, papains modified by 1,2,4-benzenetricarboxylic anhydride and pyromellitic anhydride are more stable. The immobilized papain modified by pyromellitic anhydride still retains about 40% of its activity in the thickest detergent. For the immobilized unmodified papain, the strong surfactant at 15 and 20 mg/ml causes a significant inhibition of 71% and 86%. At lower concentrations (0-10 mg/ml) of the immobilized papain modified by pyromellitic anhydride applied, there is a very slight decrease in the activity.
-
immobilization of the enzyme on Hiflow supercel, kaolinite clay, leaf mucilage, or starch gel leads to better thermal stability at 60-70C
-
immobilized enzyme does not lose any activity after tereatment with 6 M urea for 270 min, soluble papain loses 81% of its activity after urea treatment
-
immobilized enzyme is stable at 4C and pH 7.5 for up to 8 months, the soluble enzyme loses activity within 96 h
-
in the presence of 20% (w/v) sorbitol the enzyme retains nearly 65% of its activity after heating at 75C for 40 min and it retains almost 45% of its activity after heating for 80 min, the maximum effect is seen in the case of 40% (w/v) sorbitol, where the enzyme retains nearly 80 and 70% of its activity after heating at 75C for 40 and 80 min, respectively, the enzyme also shows increased thermal stability in the presence of sucrose or xylose
-
papain exists in molten globule state at pH 2.0 and in this state protein tends to aggregate in the presence of lower concentrations of guanidine hydrochloride. Such aggregation is prevented if a low concentration of urea is also present in the buffer, in addition, stabilization of the protein is also induced
-
remains fully active after prolonged exposure to 9 M urea
-
retains activity in 8 M urea
-
solid state cysteine increases the stability of n-propanol dehydrated, immobilized enzyme in in low-water tert-butanol medium
-
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
-
the operational stability, expressed as the catalytic half-life reaches about 1 week for the enzyme immobilized on the poly(glycidyl methacrylate-co-ethylene dimethylacrylate) monolith under optimal pH and temperature conditions
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acetonitrile
-
papain retains almost all its catalytic activity after 24 h of incubation in the presence of 99% (v/v) acetonitrile with a more compact conformation
dimethyl formamide
-
papain shows a complete inactivation after 24 h when exposed to those media containing 90% (v/v) dimethyl formamide because of an irreversible conformational change
Glycerol
-
in the presence of 20% (v/v) glycerol the enzyme retains nearly 80% of its activity even after heating at 75C for 40 min and it retains almost 70% of its activity even after heating for 80 min, at 30% (v/v) glycerol the enzyme retains nearly 80 and 65% of its activity after heating for 40 and 80 min, respectively at 75C
hexadecyltrimethyl ammonium bromide
-
the presence of hexadecyltrimethyl ammonium bromide allows 41% recovery of enzymatic activity of acid-unfolded papain in the presence of hexadecyltrimethyl ammonium bromide the enzyme exists as a compact intermediate with regain of native-like secondary and partial tertiary structure as well as high 8-anilino-1-naphthalene-sulfonic acid binding with the partially recovered enzymatic activity
Methanol
-
papain shows 80% loss of activity after 24 h incubation in 90% (v/v) methanol although no global conformational change and minor secondary structure rearrangements are detected
SDS
-
the presence of SDS allows 43% recovery of enzymatic activity of acid-unfolded papain, addition of 8 mM SDS results in the loss of 8-anilino-1-naphthalene-sulfonic acid binding sites exhibited by a decrease in 8-anilino-1-naphthalene-sulfonic acid fluorescence intensity, suggesting the burial of hydrophobic patches, papain at low pH and in the presence of SDS exists in a partially folded state characterized by native-like secondary structure and tertiary folds
tetrahydrofuran
-
30%, inactivation within 30 min. Sugars protect papain from tetrahydrofuran-induced inactivation in the decreasing order D-ribose, D-fructose, D-glucose, D-saccharose, D-raffinose. D-ribose at 1.6 mol per l is the most effective stabiliser. In 60% tetrahydrofuran in the presence of ribose, papain preserves about 55% of its initial activity after 2 h
Tween
-
the presence of Tween-20 allows 39% recovery of enzymatic activity of acid-unfolded papain in the presence of Tween-20, acid-unfolded papain exists as a compact intermediate with molten-globule-like characteristics
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-80C, purified enzyme can be activated to at least 65% of its original activity after storage at -80C for up to 3 months
-
4C, 60 days, the immobilized enzyme shows 20% loss of activity, the soluble enzyme shows 50% loss of activity
-
4C, protein concentration 0.04 mM, 2 mM EDTA, pH 4.3, 3% loss of activity after 48 h, 10% loss of activity after 10 days
-
4C, several months, most stable in a reversibly inactivated form, e.g. mercuripapain
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
active papain is prepared from the commercial papaya latex enzyme through affinity purification on Sepharose 4B
-
ammonium sulfate precipitation
-
aqueous two-phase system (40% (w/w) 15 mg/ml enzyme solution, 14.33-17.65% (w/w) PEG 6000, 14.27-14.42% (w/w) NaH2PO4/K2HPO4 and pH 5.77-6.3 at 20C). Propanol generates solid enzyme aggregates with almost 120% activity upon resolubilization through dilution of the precipitant
-
further purification of the commercial enzyme preparation from latex by gel filtration, to homogeneity
-
insoluble His-tagged fusion protein is solubilized and purified by nickel chelate affinity chromatography under denaturing conditions and it is further purified by gel filtration chromatography
-
purification of papain from papaya powder extracts by membranes immobilized with Reactive Red 120 or Reactive Brown 10 as dye ligands. Papain adsorption capacities for the Red 120 and Brown 10 membranes are 143.6 mg/g and 107.3 mg/g, respectively. Yields of over 80% are found for the Red 120-chitosan-nylon membrane whereas only a 50% recovery is possible using the Brown 10-CS-nylon membranes
-
purification of papain using the dye affinity membrane chromatography at pH 7.05 with Tris-HCl, papain is purified 34.6fold in a single step determined by fast protein liquid chromatography
-
recombinant enzyme
-
recombinant papain prosegment solubilized and refolded from Escherichia coli strain BL21(DE3) inclusion bodies, to homogeneity
P00784
three kinds of affinity column for the purification of papain
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DNA sequence determination and analysis of the proenzyme, expression of the isolated papain prosegment in Escherichia coli strain BL21(DE3) in the insoluble fraction
P00784
the DNA coding for propapain is cloned and expressed as inclusion bodies at a high level in Escherichia coli BL21(DE3) transformed with two T7 promoter based pET expression vectors, pET30 Ek/LIC and pET28a+, each containing the propapain gene, recombinant propapain is expressed as an insoluble His-tagged fusion protein
-
wild-type papain and D158N variant produced in a baculovirus insect cell expression system
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D158N
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clear kinetic and pH depndence differences from the wild-type enzyme
K174R
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mutation introduced according to thermostable homologue ervatamin C, unstable
K174R/V32S
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mutation introduced according to thermostable homologue ervatamin C, improvement of thermal stability
K174R/V32S/G36S
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mutation introduced according to thermostable homologue ervatamin C, improvement of thermal stability
V133A/S205E
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change in specificity compared to wild-type enzyme
V133A/V157G/S205E
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important decrease in activity, change in specificity compared to the wild-type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acid-unfolded papain in the presence of 8 mM SDS and 3.5 mM hexadecyltrimethyl ammonium bromide retains its partial tertiary structure
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fractions containing propapain are pooled and refolded by rapid dilution into a refolding buffer at pH 8.6, the denatured protein folds best at pH 8.5 and at 4C, while pH values above 8.8 and below 7.0 are not suitable for folding, folding process requires addition of 0.5 M arginine, 1 mM glutathione, 0.1 mM GSSG and 15% glycerol
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recombinant papain prosegment from Escherichia coli strain BL21(DE3) inclusion bodies by 2% Triton X-100, 8 M guanidinium hydrochloride, and dialysis against 50 mM phosphoric acid/NaOH buffer, pH 7.0, and centrifugation at 45000 rpm for 1 h
P00784
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
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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
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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
analysis
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use of the enzyme in sequence determination
biotechnology
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immobilization of papain and dehydration by n-propanol in low-water media at pH 6.4 and 25C in 150 mM sodium phosphate buffer, stability is increased by solid state cysteine, overview
biotechnology
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papain immobilization on magnetic composite microspheres at pH 8.0 and 30C, quantification and kinetics, overview, the immobilized enzyme exhibits better environmentally adaptability and reusability than the soluble enzyme
biotechnology
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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
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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
industry
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the cotton fabric immobilized modified papain has potential applicationsin the functional textiles field
industry
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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
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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
medicine
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enzyme is used for a number of biomedical applications
medicine
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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
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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
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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
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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
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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
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used for wound debridement, the removal of necrotic tissue
medicine
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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
nutrition
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used extensively in food processing especially in tenderization of meat
nutrition
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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
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papain is used in the preparation of fish protein concentrates from fish waste; production of dehydrated pulses and beans; the enzyme is used for the development of roast beef-like flavours by partial hydrolysis of proteins; 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
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chill-proofing ability in beer
synthesis
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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
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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 80C 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
synthesis
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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 55C and pH 5.6, the transformation yield is 99.5%
synthesis
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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
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use as catalyst in asymetric synthesis of acyl derivatives and in peptide synthesis