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Information on EC 3.4.22.2 - papain and Organism(s) Carica papaya and UniProt Accession P00784
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3.4.22.2 papainSpecify your search results
Word Map
- 3.4.22.2
- cathepsins
- proteinases
- chymotrypsin
- pepsin
- cystatins
- bromelain
- igg
- hydrolysates
- cartilage
- immunoglobulin
- ficin
- pronase
- proteoglycans
- erythrocyte
- glycosaminoglycans
- alpha-chymotrypsin
- elastase
- neuraminidase
- chondroitin
- alcalase
- subtilisin
- latex
- thermolysin
- carica
- allergen
-
articular
-
agglutination
- collagenase
- emphysema
- plasmin
- kininogens
-
fab\'2
-
anti-d
-
intra-articular
-
bacteriocins
- pineapple
- legumains
-
l-like
- pancreatin
- meromyosin
- dermatan
-
emphysematous
- chondroitinase
-
antiglobulin
- nutrition
-
actin-activated
- medicine
- food industry
-
enzyme-treated
- industry
-
alloantibody
-
subfragment-1
- analysis
- synthesis
-
carlsberg
- biotechnology
-
procathepsins
The taxonomic range for the selected organisms is: Carica papaya
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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'
Synonyms
papain, papaine, adolph's meat tenderizer, papaya peptidase i, papaya proteinase i, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Adolph's Meat Tenderizer
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-
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arbuz
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-
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enzeco papain
-
-
-
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papain
-
-
papaine
-
-
-
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papaya peptidase I
-
-
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papayotin
-
-
-
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PPI
-
-
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summetrin
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-
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velardon
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
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'
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
9001-73-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
benzyloxycarbonyl-Ala-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Ala-4-aminoantipyrine + methanol
-
-
-
?
benzyloxycarbonyl-Gly-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Gly-4-aminoantipyrine + methanol
-
-
-
?
benzyloxycarbonyl-Ser-OMe + 4-aminoantipyrine
benzyloxycarbonyl-Ser-4-aminoantipyrine + methanol
-
-
-
?
carboxybenzoyl-Phe-Arg-7-(4-methyl)coumarylamide + H2O
carboxybenzoyl-Phe-Arg + 7-amino-4-methylcoumarin
fluorogenic substrate
-
-
?
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
-
-
?
Nalpha-benzoyl-DL-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
?
tarocystatin + H2O
?
the C-terminal cystatin-like extension of tarocystatin is easily digested by papain
-
-
?
(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 + 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
-
-
-
-
?
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-L-Phe-Gly-4-nitroanilide + H2O
acetyl-L-Phe-Gly + 4-nitroaniline
-
-
-
-
?
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-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-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-nitroanilide + H2O
benzyloxycarbonyl-Phe-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-Phe-Leu-4-nitroanilide + H2O
benzyloxycarbonyl-Phe-Leu + 4-nitroaniline
-
-
-
-
?
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
-
?
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
-
-
?
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
-
?
hippuric acid + aniline
hippuryl anilide
-
weak activity, 0.1% of the hydrolytic activity with N-benzoyl-L-argininamide
-
r
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-Pro-L-Phe-L-Leu-4-nitroanilide + H2O
L-Pro-L-Phe-L-Leu + 4-nitroaniline
-
-
-
-
?
lambda repressor + H2O
?
-
no cleavage of the operator-bound repressor dimer
-
?
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-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-benzoyl-Arg-p-nitroanilide + H2O
Nalpha-benzoyl-Arg + p-nitroaniline
-
-
-
?
N-benzoyl-DL-arginine-2-naphthylamide + H2O
N-benzoyl-DL-arginine + 2-naphthylamine
-
-
-
-
?
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
-
-
-
-
?
Nalpha-benzoyl-Arg-p-nitroanilide + H2O
Nalpha-benzoyl-Arg + p-nitroaniline
-
-
-
?
Nalpha-benzoyl-DL-arginine-4-nitroanilide + H2O
Nalpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-Benzoyl-L-Arg ethyl ester + H2O
?
-
-
-
-
?
phthalyl-Phe-Leu-p-nitroanilide + H2O
phthalyl-Phe-Leu + 4-nitroaniline
-
-
-
?
succinyl-Phe-Leu-4-nitroanilide + H2O
succinyl-Phe-Leu + 4-nitroaniline
-
-
-
-
?
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
?
-
molecular recognition of mature enzyme and prosegment, overview
-
-
?
additional information
?
-
papain is the founding member of the large C1 family of papain-like cysteine proteases
-
-
?
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
?
-
-
enzyme catalyses the hydrolysis of peptide bonds of basic amino acids, such as leucine or glycine
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
tarocystatin + H2O
?
the C-terminal cystatin-like extension of tarocystatin is easily digested by papain
-
-
?
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
-
-
?
additional information
?
-
papain is the founding member of the large C1 family of papain-like cysteine proteases
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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+
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)
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
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)
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)
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
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+
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)
tarocystatin
the N-terminal cystatin domain (residues 1-98) of tarocystatin has inhibitory ability against 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)
(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
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
Ba2+
-
residual activity in the presence of 20 mM: 13% free papain, 38% immobilized papain
barley cystatin protease inhibitor
-
inhibited by various cystatin vatiants, HvCPI-1, HvCPI-2, HvCPI-3, HvCPI-4, HvCPI-5, HvCPI-6
-
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-Phe-Ala-glyoxal
-
competitive, 13C-NMR study of the inhibition
Ca2+
-
residual activity in the presence of 20 mM: 10% free papain, 48% immobilized papain
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
-
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
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
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
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
-
methanol
-
number of papain active sites decreases with increase of inhibitor concentration
Mg2+
-
residual activity in the presence of 20 mM: 20% free papain, 57% immobilized papain
Mn2+
-
residual activity in the presence of 20 mM: 0% free papain, 18% immobilized papain
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
-
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
Zn2+
-
residual activity in the presence of 20 mM: 0% free papain, 16% immobilized papain
additional information
loosely packed papain prosegment displays inhibitory activity but can also function as activator for the mature enzyme, overview
-
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
-
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
-
no inhibition by synthetic cyclic peptide CTSPRLHPCGGGS-NH2, interaction anaylsis of enzyme with diverse synthetic peptides in a phage display assay, 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
COMMENTARY
LITERATURE
IMAGE
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 50°C
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
2-mercaptopropionic acid
-
required, complete activation at 0.05 N when the enzyme concentration is 0.49 mM
additional information
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
1.8
benzyloxycarbonyl-L-citrullyl-L-Arg 4-methylcoumarin-7-amide
-
mutant enzyme D158N
0.00212
N-alpha-benzyloxycarbonyl-L-lysine 4-nitrophenyl ester
-
pH 6.5, 27°C, Vmax: 2.14 miroM/sec
0.00079
casein
enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide, 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
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
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
0.191
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
0.00057
casein
-
papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22°C
0.00385
Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans
-
pH 6.8, 40°C, in presence of 1% methanol
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
-
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
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
thermodynamics of the thermal unfolding of the recombinant prosegment, overview, pH-jump kinetics of the prosegment, overview
-
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
-
Km (casein) for immobilized papain is lower than for free papain
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0102
casein
enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide, 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
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
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
0.00000035
casein
-
papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22°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
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
additional information
additional information
-
kcat (casein) for immobilized papain is much lower than for free papain
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
230.8
casein
enzyme immobilized on multi-walled carbon nanotubes, pH 7.5, 23°C
0.00061
casein
-
papain immobilized on sepharose 6B in presence of 200 mM cysteine, pH 7.5, 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000000036
chagasin
inactivation of papain is very fast, rate constant for inactivation is 1500 mM/s
-
0.0000019
papain prosegment
recombinant prosegment, pH 7.0, 20°C, inhibition kinetics
-
0.00000001
cystatin SN, cystatin SN variant G12A/G13A, cystatin SN variant P106G/W107G
-
below
-
additional information
additional information
-
inhibition constants for various barley cystatin protease inhibitor variants
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
(eta5-C5H5)Fe(CO)3 eta1-N-succinimidato
Carica papaya
-
pH 6.5, temperature not specified in the publication
-
0.28
(eta5-C5H5)Mo(CO)3 eta1-N-succinimidato
Carica papaya
-
pH 6.5, temperature not specified in the publication
-
0.48
(eta5-C5H5)W(CO)3 eta1-N-succinimidato
Carica papaya
-
pH 6.5, temperature not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.205
substrate: casein, enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide, pH 7.5, 23°C
125.9
recombinant papain, in 100 mM sodium acetate and 2 mM EDTA at pH 6.5
221.7
commercial papain, in 100 mM sodium acetate and 2 mM EDTA at pH 6.5
0.059
-
activity of immobilized papain dehydrated by n-propanol in low-water tert-butanol media
additional information
additional information
-
1,2,4-benzenetricarboxylic papain has 97.73% relative activity compared to the unmodified enzyme
additional information
1,2,4-benzenetricarboxylic papain has 97.73% relative activity compared to the unmodified enzyme
additional information
-
pyromellitic papain has 95.88% relative activity compared to the unmodified enzyme
additional information
pyromellitic papain has 95.88% relative activity compared to the unmodified enzyme
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
-
activity decreases with increasing ethanol content, papain from papaya latex is less sensitive to ethanol
additional information
-
Papain from latex shows a significantly higher and stable catalytic activityrespect to fruit papain
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
enzyme modified by 1,2,4-benzenetricarboxylic anhydride or pyromellitic anhydride
6.5
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 39°C, 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.
7.5
additional information
8
enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide
8
-
enzyme immobilized on sepharose 6B in presence or absence of 200 mM cysteine
9
1,2,4-benzenetricarboxylic-modified and pyromellitic acid-modified enzyme immobilized on cotton fabric
additional information
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
ORGANISM
UNIPROT
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 - 12
pH 4.0: about 55% of maximal activity, pH 12.0: about 45% of maximal activity, enzyme immobilized on multi-walled carbon nanotubes
4 - 9
pH 4.0: about 50% of maximal activity, pH 9.0: about 35% of maximal activity, soluble enzyme
6.4 - 10.2
pH 6.4: about 85% of maximal activity, pH 10.2: about 70% of maximal activity
6.4 - 9.4
pH 6.4: about 85% of maximal activity, pH 9.4: about 50% of maximal activity
5 - 8
-
pH 5.0: about 70% of maximal activity, pH 8.0: about 85% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
80
20
37
40
60
65
75
80
additional information
-
temperature-dependences of the second-order rate constants of the reaction involving the catalytic site thiol, overview, stopped-flow method
80
the activity of immobilized pyromellitic papain has a vital peak at 80°C, which may be attributed largely to the particular enzyme structure
80
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 80°C
80
enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide
80
-
enzyme immobilized on sepharose 6B in presence or absence of 200 mM cysteine
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 70
25°C: about 65% of maximal activity, 70°C: about 60% of maximal activity, soluble enzyme
25 - 90
25°C: about 50% of maximal activity, 90°C: about 70% of maximal activity, papain immobilized on hybrid nanoflowers
30 - 70
30°C: about 65% of maximal activity, 70°C: about 80% of maximal activity, soluble enzyme
30 - 80
30°C: about 40% of maximal activity, 80°C: about 80% of maximal activity, enzyme immobilized on multi-walled carbon nanotubes
60 - 80
the activity of immobilized unmodified papain and immobilized benzenetricarboxylic papain are increased stably over a period of 60 to 80°C without significant change
25 - 70
-
25°C: about 65% of maximal activity, 70°C: about 60% of maximal acticity
50 - 100
-
50°C: about 35% of maximal activity, 100°C: about 95% of maximal activity, immobilized enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
green fruit skin has the highest enzyme content, ripening decreases the enzyme level
additional information
Papaya latex is usually harvested from fruit skin of green papaya fruits by mechanical wounding
-
-
81552, 95671, 95675, 95676, 95681, 95685, 95702, 95705, 95706, 95707, 649521, 649585, 650312, 653025, 667306, 667511, 677395, 678470, 678740, 678751, 679221, 681479, 718263, 718346, 733086
additional information
gene expression patterns of the papaya PLCP genes in different tissues are assessed by transcriptome sequencing and quantitative RT-PCR. Most of the papaya PLCP genes of subfamily III are expressed at high levels in leaf and green fruit tissues
additional information
-
gene expression patterns of the papaya PLCP genes in different tissues are assessed by transcriptome sequencing and quantitative RT-PCR. Most of the papaya PLCP genes of subfamily III are expressed at high levels in leaf and green fruit tissues
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
all four major papain-like cysteine proteases (PLCPs) purified from papaya latex, including papain, chymopapain, glycyl endopeptidase and caricain, are grouped into the lineage-specific expansion branch in the subfamily III of papain-like cysteine proteases (PLCPs). Tandem duplications play the dominant role in affecting copy number of PLCPs in plants. Significant variations in size of the PLCP subfamilies among species may reflect genetic adaptation of plant species to different environments. The lineage-specific expansion of papaya PLCPs of subfamily III might have been promoted by the continuous reciprocal selective effects of herbivore attack and plant defense. Phylogenetic analysis, conserved domain identification, gene duplication analysis, and chromosomal distribution of PLCPs, overview
metabolism
papain-like cysteine proteases (PLCPs), a large group of cysteine proteases structurally related to papain, play important roles in plant development, senescence, and defense responses
physiological function
-
papain displays a strong anti-angiogenic effect in VEGF activated HUVEC human umbilical vein endothelial cells in vitro
additional information
adsorption properties of protein papain at the solid/liquid interfaces of different hydrophobicity (highly oriented pyrolytic graphite (HOPG), bare gold, CH3, OH, and COOH-terminated self-assembled monolayers on gold) are studied by a combined quartz crystal microbalance and atomic force microscopy techniques. Papain forms an incomplete monolayer at hydrophobic interfaces (HOPG and CH3-terminated substrate), whereas on more hydrophilic ones, a complete monolayer formation is always observed with either the onset of the formation of a second layer (bare gold substrate) or adsorption in a multilayer fashion, possibly a bilayer formation (OH-terminated substrate). The surface concentration and compact monolayer film thickness is much lower on the COOH-terminated substrate compared to other surfaces studied. This result is explained by partial dissociation of the interfacial COOH groups leading to additional electrostatic interactions between the positively charged protein domains and negatively charged carboxylate anions, as well as to local pH changes promoting protein denaturation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PAPA1_CARPA
345
1
38922
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 50°C indicating that processing of propapain to papain occurs in a stepwise manner
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the papain prosegment shows a high degree of conformational flexibility, proenzyme structure molecular modeling
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
side-chain modification
proteolytic modification
the proenzyme is activated by cleavage of the prosegment
proteolytic modification
the zymogen of papain contains a pro-peptide at the N-terminus of the catalytic domain. Pro-peptide contains residues which act as pH-sensors in zymogen activation cascade. The conserved Asp72 residue of the pro-peptide, is a highly conserved residue of the GXNXFXD motif that is an important pH sensor in the zymogen activation process and the pro-peptide part can also be a useful target of protein engineering for altering the activation pH of a protease
side-chain modification
-
propapain is activated by intramolecular thiol-disulfide exchange which is catalyzed by cysteine
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
LITERATURE
a complex of chagasin, a protein inhibitor from Trypanosoma cruzi, and papain is crystallized by using the hanging-drop vapor diffusion method at 18°C, 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
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
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
-
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-inhibitor complex with benzyloxycarbonyl-Leu-Leu-leucinal or benzyloxycarbonyl-L-Leu-L-Leu methoxymethyl ketone
-
structure of papain complexed with benzyloxycarbonyl-L-Phe-L-Ala-L-Ala chloromethylketone
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D72A
the mutant undergoes autoactivation at pH 5.0 compared to pH 4.0 for wild-type enzyme. The general proteolytic activity of the D72A mutant remains similar to that of wild-type
K174R
-
mutation introduced according to thermostable homologue ervatamin C, unstable
K174R/V32S
-
mutation introduced according to thermostable homologue ervatamin C, improvement of thermal stability
K174R/V32S/G36S
-
mutation introduced according to thermostable homologue ervatamin C, improvement of thermal stability
V133A/V157G/S205E
-
important decrease in activity, change in specificity compared to the wild-type enzyme
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
after 60 min of incubation the immobilized enzyme retains about 98% of its residual activity
753834
3
after 60 min of incubation the immobilized enzyme retains about 53% of its residual activity
753834
4 - 10
the enzyme retains more than 80% of initial activity after 30 min incubation at pH 3.0-10.0
752461
6 - 11
the native enzyme rapidly decreases to the relative activity of 70%
695700
7 - 10
1 - 2
-
half life after 60 storage: below 5% free papain, 40% immobilized papain
733073
7 - 10
the papain modified by by 1,2,4-benzenetricarboxylic anhydride and pyromellitic anhydride displaying over 80% of its activity
695700
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
678740
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
80
90
22
40
50
-
oxidized, inactive enzyme, in absence of activator, 67% of the initial activity remains after 28 days
56
-
at pH 2.0, partially reduced papain, single cooperative transition with a midpoint at 55.61°C
60
65
70
75
80
90
additional information
55
390 min, the soluble enzyme retains 41.9% of its activity, enzyme immobilized on hybrid nanoflowers retains 77.2% of its activity
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
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
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
40
-
single disulfide reduced carboxymethylated papain, at neutral pH, the protein started unfolding after 40°C
60
-
half-life of wild-type, mutant K174R/V32S and mutant K174R/V32S/G36S is 77, 114, and 171 min, respectively
65
-
half-life of wild-type, mutant K174R/V32S and mutant K174R/V32S/G36S is 35, 45, and 80 min, respectively
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
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
-
immobilized enzyme loses 66% of its activity after 300 min incubation at 75°C
additional information
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
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
compared to free papain, the enzyme non-covalently immobilized on multi-walled carbon nanotubes exhibits significantly improved thermal, pH and recycling stability
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 45°C, 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 papain by covalent attachment on Sepharose 6B activated by using cyanogen bromide brings about significant enhancement of storage and thermal stability and of stability at extreme pHs
papain immobilized on hybrid nanoflowers retains 88.8% of its initial activity after ten successive cycles of reuse
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 75°C, papain immobilized on the poly(glycidyl methacrylate-co-ethylene dimethylacrylate) monolith loses 10% of its activity
-
immobilization of the enzyme on Hiflow supercel, kaolinite clay, leaf mucilage, or starch gel leads to better thermal stability at 60-70°C
-
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 4°C 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 75°C 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 75°C 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
-
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
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 75°C 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 75°C
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
LITERATURE
-80°C, purified enzyme can be activated to at least 65% of its original activity after storage at -80°C for up to 3 months
23°C, pH 7.5, the enzyme immobilized on multi-walled carbon nanotubes loses about 20% of its activity after 40 days, the soluble enzyme loses about 40% of its activity after 20 days
4°C, pH 7.5, the enzyme immobilized on multi-walled carbon nanotubes is stable for 60 days, the soluble enzyme loses about 65% of its activity after 60 days
25°C, model wine (pH 3.2, 12% ethanol), 7 days, papain from papaya latex retains 50% of activity and papain from ripe fruit retains 18% activity
-
4°C, 60 days, the immobilized enzyme shows 20% loss of activity, the soluble enzyme shows 50% loss of activity
-
4°C, 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
-
4°C, several months, most stable in a reversibly inactivated form, e.g. mercuripapain
-
after 15 days, free papain retains 31% of its initial activity,whereas the immobilized papain retains 40% of initial activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
active papain is prepared from the commercial papaya latex enzyme through affinity purification on Sepharose 4B
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
recombinant papain prosegment solubilized and refolded from Escherichia coli strain BL21(DE3) inclusion bodies, to homogeneity
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 20°C). 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
-
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
-
using dye ligand affinity chromatography with a cryogel column. Papain is purified 42fold in single step
-
CLONED (Commentary)
ORGANISM
UNIPROT
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
gene CpXCP5, genotyping using the peptidase_C1 domain, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis
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
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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 4°C, 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
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
acid-unfolded papain in the presence of 8 mM SDS and 3.5 mM hexadecyltrimethyl ammonium bromide retains its partial tertiary structure
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
food industry
combination of ultrasound and papain is more beneficial for improving functional properties of meat compared with the individual treatment
industry
medicine
analysis
biotechnology
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
medicine
nutrition
synthesis
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
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
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
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
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
-
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
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
-
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
nutrition
-
papain is used in the preparation of fish protein concentrates from fish waste
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vartak, H.G.; Rele, M.V.; Jagannathan, V.
Proteinase inhibitors from Vigna unguiculata subsp. cylindrica. III. Properties and kinetics of inhibitors of papain, subtilisin, and trypsin
Arch. Biochem. Biophys.
204
134-140
1980
Carica papaya
Dubois, T.; Jacquet, A.; Schnek, A.G.; Looze, Y.
The thiol proteinases from the latex of Carica papaya L. I. Fractionation, purification and preliminary characterization
Biol. Chem. Hoppe-Seyler
369
733-740
1988
Carica papaya
Glazer, A.N.; Smith, E.L.
Papain and other plant sulfhydryl proteolytic enzymes
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
3
501-546
1971
Carica papaya
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Saito, M.; Kawaguchi, N.; Hashimoto, M.; Kodama, T.; Higuchi, N.; Tanaka, T.; Nomoto, K.; Murachi, T.
Purification and structure of novel cysteine proteinase inhibitors, staccopins P1 and P2, from Staphylococcus tanabeensis
Agric. Biol. Chem.
51
861-868
1987
Carica papaya
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Abe, K.; Emori, Y.; Kondo, H.; Arai, S.; Suzuki, K.
The NH2-terminal 21 amino acid residues are not essential for the papain-inhibitory activity of oryzacystatin, a member of the cystatin superfamily. Expression of oryzacystatin cDNA and its truncated fragments in Escherichia coli
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1988
Carica papaya
Groeger, U.; Stehle, P.; Furst, P.; Leuchtenberger, W.; Drauz, K.
Papain-catalyzed synthesis of dipeptides
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187-198
1989
Carica papaya
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Cohen, L.W.; Coghlan, V.M.; Dihel, L.C.
Cloning and sequencing of papain-encoding cDNA
Gene
48
219-227
1986
Carica papaya
Chiou, R.Y.Y.; Beuchat, L.R.
Characteristics and application of immobilized papain in a continuous-flow reactor
Biotechnol. Appl. Biochem.
8
529-536
1986
Carica papaya
Storer, A.; Carey, P.R.
Comparison of the kinetics and mechanism of the papain-catalyzed hydrolysis of esters and thiono esters
Biochemistry
24
6808-6818
1985
Carica papaya
Syu, W.J.; Wu, S.H.; Wang, K.T.
Purification of papain by affinity chromatography
J. Chromatogr.
262
346-351
1983
Carica papaya
Kilara, A.; Shahani, K.M.; Wagner, F.W.
Preparation and properties of immobilized papain and lipase
Biotechnol. Bioeng.
14
1703-1714
1977
Carica papaya
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Messing, R.A.
Insoluble papain prepared by adsorption on porous glass
Enzymologia
38
39-42
1970
Carica papaya
Burke, D.E.; Lewis, S.D.; Shafer, J.A.
A two-step procedure for purification of papain from extract of papaya latex
Arch. Biochem. Biophys.
164
30-36
1974
Carica papaya
Drenth, J.; Jansonius, J.N.; Koekoek, R.; Wolters, B.G.
Papain, X-ray structure
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
3
485-499
1971
Carica papaya
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Skelton, G.S.
Papaya proteinases. III. Effect of activators on the hydrolysis of benzoyl argininamide
Enzymologia
35
279-282
1968
Carica papaya
Matsumoto, K.; Murata, M.; Sumiya, S.; Mizoue, K.; Kitamura, K.; Ishida, T.
X-ray crystal structure of papain complexed with cathepsin B-specific covalent-type inhibitor: substrate specificity and inhibitory activity
Biochim. Biophys. Acta
1383
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1998
Carica papaya
Sueyoshi, T.; Enjyoji, K.; Shimada, T.; Kato, H.; Iwanaga, S.; Bando, Y.; Kominami, E.; Katunuma, N.
A new function of kininogens as thiol-proteinase inhibitors: inhibition of papain and cathepsins B, H and L by bovine, rat and human plasma kininogens
FEBS Lett.
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193-195
1985
Carica papaya
Mitchell, R.E.J.; Chaiken, I.M.; Smith, E.L.
The complete amino acid sequence of papain. Additions and corrections
J. Biol. Chem.
245
3485-3492
1970
Carica papaya
Blumberg, S.; Schechter, I.; Berger, A.
The purification of papain by affinity chromatography
Eur. J. Biochem.
15
97-102
1970
Carica papaya
Fink, A.L.; Bender, M.L.
Binding sites for substrate leaving groups and added nucleophiles in papain-catalyzed hydrolyses
Biochemistry
8
5109-5118
1969
Carica papaya
Menard, R.; Storer, A.C.
Papain
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Carica papaya
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Skelton, G.S.
Papaya proteinases. I. Temperature-and pH-stability curves
Enzymologia
35
270-274
1968
Carica papaya
Skelton, G.S.
Papaya proteinases. II. Effect of ascorbic acid on proteolytic activity
Enzymologia
35
275-278
1968
Carica papaya
Sluyterman, L.A.AE.
Product inhibition of papain action
Biochim. Biophys. Acta
85
316-321
1964
Carica papaya
Sluyterman, L.A.AE.
Kinetics of the hydrolysis of benzoylglycine ethyl ester catalyzed by papain
Biochim. Biophys. Acta
85
305-315
1964
Carica papaya
Baker, E.; Drenth, J.
The thiol proteases: structure and mechanism
Biological Macromolecules and Assemblies (Junak, F. McPherson eds. )
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1987
Carica papaya
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Smyth, D.G.
Use of papain, pepsin, and subtilisin in sequence determination
Methods Enzymol.
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1967
Carica papaya
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Schrder, E.; Phillips, C.; Garman, E.; Harlos, K.; Crawford, C.
X-ray crystallographic structure of a papain-leupeptin complex
FEBS Lett.
315
38-42
1993
Carica papaya
Carty, R.P.; Kirschenbaum, D.M.
The papain-catalyzed synthesis of hippuryl anilide
Biochim. Biophys. Acta
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446-461
1964
Carica papaya
Kim, M.J.; Yamamoto, D.; Matsumoto, K.; Inoue, M.; Ishida, T.; Mizuno, H.; Sumiya, S.; Kitamura, K.
Crystal structure of papain-E64-c complex. Binding diversity of E64-c to papain S2 and S3 subsites
Biochem. J.
287
797-803
1992
Carica papaya
Stubbs, M.T.; Laber, B.; Bode, W.; Huber, R.; Jerala, R.; Lenaricic, B.; Turk, V.
The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction
EMBO J.
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1939-1947
1990
Carica papaya
Mekkes, J.R.; le Poole, I.C.; Das, P.K.; Kammeyer, A.; Westerhof, W.
In vitro tissue-digesting properties of krill enzymes compared with fibrinolysin/DNAse, papain and placebo
Int. J. Biochem. Cell Biol.
29
703-706
1997
Carica papaya
Yamamoto, A.; Tomoo, K.; Doi, M.; Ohishi, H.; Inoue, M.; Ishida, T.; Yamamoto, D.; Tsuboi, S.; Okamoto, H.; Okada, Y.
Crystal structure of papain-succinyl-Gln-Val-Val-Ala-Ala-p-nitroanilide complex at 1.7-A resolution: noncovalent binding mode of a common sequence of endogenous thiol protease inhibitors
Biochemistry
31
11305-11309
1992
Carica papaya
Yamamoto, D.; Ishida, T.; Inoue, M.
A comparison between the binding modes of a substrate and inhibitor to papain as observed in complex crystal structures
Biochem. Biophys. Res. Commun.
171
711-716
1990
Carica papaya
Menard, R.; Khouri, H.E.; Plouffe, C.; Dupras, R.; Ripoll, D.; Vernet, T.; Tessier, D.C.; Laliberte, F.; Thomas, D.Y.; Storer, A.C.
A protein engineering study of the role of aspartate 158 in the catalytic mechanism of papain
Biochemistry
29
6706-6713
1990
Carica papaya
Khouri, H.E.; Vernet, T.; Menard, R.; Parlati, F.; Laflamme, P.; Tessier, D.C.; Gour-Salin, B.; Thomas, D.Y.; Storer, A.C.
Engineering of papain
Biochemistry
30
8929-8936
1991
Carica papaya
Matsumoto, K.; Murata, M.; Sumiya, S.; Kitamura, K.; Ishida, T.
Clarification of substrate specificity of papain by crystal analyses of complexes with covalent-type inhibitors
Biochim. Biophys. Acta
1208
268-276
1994
Carica papaya
Kozak, M.; Kozian, E.; Gronka, Z.; Jaskolski, M.
Crystallization and preliminary crystallographic studies of a new form of papain from Carica papaya
Acta Biochim. Pol.
44
601-606
1997
Carica papaya
LaLonde, J.M.; Zhao, B.; Smith, W.W.; Janson, C.A.; DesJarlais, R.I.; Tomaszek, T.A.; Carr, T.J.; Thompson, S.K.; Oh, H.; Yamashita, D.N.; Veber, D.F.; Abdel-Meguid, S.S.
Use of papain as a model for the structure-based design of cathepsin K inhibitors: crystal structures of two papain-inhibitor complexes demonstrate binding to S'-subsites
J. Med. Chem.
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4567-4576
1998
Carica papaya
Inman, F.P.; Hazen, S.R.
Characterization of a large fragment produced by proteolysis of human immunoglobulin M with papain
J. Biol. Chem.
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5598-5604
1968
Carica papaya
Brocklehurst, K.; Carlsson, J.; Kierstan, M.P.J.; Crok, E.M.
Covalent chromatography by thiol-disulfide interchange
Methods Enzymol.
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532-544
1974
Carica papaya
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Brocklehurst, K.; Carlsson, J.; Kierstan, M.P.J.; Crook, E.M.
Covalent chromatography. Preparation of fully active papain from dried papaya latex
Biochem. J.
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573-584
1973
Carica papaya
Brocklehurst, K.; Baines, B.S.; Kierstan, M.P.J.
Papain and other constituents of Carica papaya L
Top. Enzyme Ferment. Biotechnol.
5
262-335
1981
Carica papaya
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Kennedy, J.F.; Pike, V.W.
Papain, chymotrypsin and related proteins - a comparative study of their beer chill-proofing abilities and characteristics
Enzyme Microb. Technol.
3
59-63
1981
Carica papaya
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Abernethy, J.L.; Lovett, C.M.; Haddad, A.; Felberg, J.D.
Stereoselective action of acylated crude papain toward mandelic and atrolactic hydrazides
Bioorg. Chem.
11
251-261
1982
Carica papaya
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Szabelski, M.; Stachowiak, K.; Wiczk, W.
Influence of organic solvents on papain kinetics
Acta Biochim. Pol.
48
1197-1201
2001
Carica papaya
Szabelski, M.; Stachowiak, K.; Wiczk, W.
Influence of Me2SO and incubation time on papain activity studied using fluorogenic substrates
Acta Biochim. Pol.
48
995-1002
2001
Carica papaya
Tseng, C.C.; Tseng, C.P.; Levine, M.J.; Bobek, L.A.
Differential effect toward inhibition of papain and cathepsin C by recombinant human salivary cystatin SN and its variants produced by a baculovirus system
Arch. Biochem. Biophys.
380
133-140
2000
Carica papaya
Achilles, K.; Schirmeister, T.; Otto, H.H.
beta-Lactam derivatives as enzyme inhibitors: 1-peptidyl derivatives of 4-phenylazetidin-2-one as inhibitors of elastase and papain
Arch. Pharm.
333
243-253
2000
Carica papaya
Edwin, F.; Sharma, Y.V.; Jagannadham, M.V.
Stabilization of molten globule state of papain by urea
Biochem. Biophys. Res. Commun.
290
1441-1446
2002
Carica papaya
Lowther, J.; Djurdjevic-Pahl, A.; Hewage, C.; Malthouse, J.P.
A 13C-NMR study of the inhibition of papain by a dipeptide-glyoxal inhibitor
Biochem. J.
366
983-987
2002
Carica papaya
Theodorou, L.G.; Lymperopoulos, K.; Bieth, J.G.; Papamichael, E.M.
Insight into the catalysis of hydrolysis of four newly synthesized substrates by papain: a proton inventory study
Biochemistry
40
3996-4004
2001
Carica papaya
Hwang, S.R.; Steineckert, B.; Toneff, T.; Bundey, R.; Logvinova, A.V.; Goldsmith, P.; Hook, V.Y.
The novel serpin endopin 2 demonstrates cross-class inhibition of papain and elastase: localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells
Biochemistry
41
10397-10405
2002
Carica papaya
Edwin, F.; Jagannadham, M.V.
Single disulfide bond reduced papain exists in a compact intermediate state
Biochim. Biophys. Acta
1479
69-82
2000
Carica papaya
Xian, M.; Chen, X.; Liu, Z.; Wang, K.; Wang, P.G.
Inhibition of papain by S-nitrosothiols. Formation of mixed disulfides
J. Biol. Chem.
275
20467-20473
2000
Carica papaya
Ghosh, K.; Chattopadhyaya, R.
Papain does not cleave operator-bound lambda repressor: structural characterization of the carboxy terminal domain and the hinge
J. Biomol. Struct. Dyn.
18
557-567
2001
Carica papaya
Luo, Q.; Mao, X.; Kong, L.; Huang, X.; Zou, H.
High-performance affinity chromatography for characterization of human immunoglobulin G digestion with papain
J. Chromatogr. B
776
139-147
2002
Carica papaya
Golan, R.; Zehavi, U.; Naim, M.; Patchornik, A.; Smirnoff, P.; Herchman, M.
Inhibition of Papaya latex papain by photosensitive inhibitors. 1-(4,5-dimethoxy-2-nitrophenyl)-2-nitroethene and 1,1-dicyano-2-(4,5-dimethoxy-2-nitrophenyl)-ethene
J. Protein Chem.
19
117-122
2000
Carica papaya
Kaul, P.; Sathish, H.A.; Prakash, V.
Effect of metal ions on structure and activity of papain from Carica papaya
Nahrung
46
2-6
2002
Carica papaya
Achilles, K.; Schneider, M.; Schirmeister, T.; Otto, H.H.
beta-Lactam derivatives as enzyme inhibitors: N-substituted derivatives of (S)-4-oxoazetidine-2-carboxylate as inhibitors of elastase and papain
Pharmazie
55
798-802
2000
Carica papaya
Sharma, Y.V.; Jagannadham, M.V.
N-terminal domain unfolds first in the sequential unfolding of papain
Protein Pept. Lett.
10
83-90
2003
Carica papaya
Franco, O.L.; Grossi de Sa, M.F.; Sales, M.P.; Mello, L.V.; Oliveira, A.S.; Rigden, D.J.
Overlapping binding sites for trypsin and papain on a Kunitz-type proteinase inhibitor from Prosopis juliflora
Proteins Struct. Funct. Genet.
49
335-341
2002
Carica papaya
Naeem, A.; Khan, K.A.; Khan, R.H.
Characterization of a partially folded intermediate of papain induced by fluorinated alcohols at low pH
Arch. Biochem. Biophys.
432
79-87
2004
Carica papaya
Gutierrez-Gonzalez, L.H.; Rojo-Dominguez, A.; Cabrera-Gonzalez, N.E.; Perez-Montfort, R.; Padilla-Zuniga, A.J.
Loosely packed papain prosegment displays inhibitory activity
Arch. Biochem. Biophys.
446
151-160
2006
Carica papaya (P00784)
Bratkovic, T.; Lunder, M.; Popovic, T.; Kreft, S.; Turk, B.; Strukelj, B.; Urleb, U.
Affinity selection to papain yields potent peptide inhibitors of cathepsins L, B, H, and K
Biochem. Biophys. Res. Commun.
332
897-903
2005
Carica papaya
Vishu Kumar, A.B.; Varadaraj, M.C.; Gowda, L.R.; Tharanathan, R.N.
Characterization of chito-oligosaccharides prepared by chitosanolysis with the aid of papain and pronase, and their bactericidal action against Bacillus cereus and Escherichia coli
Biochem. J.
391
167-175
2005
Carica papaya
Gul, S.; Mellor, G.W.; Thomas, E.W.; Brocklehurst, K.
Temperature-dependences of the kinetics of reactions of papain and actinidin with a series of reactivity probes differing in key molecular recognition features
Biochem. J.
396
17-21
2006
Carica papaya
Valente, C.; Guedes, R.C.; Moreira, R.; Iley, J.; Gut, J.; Rosenthal, P.J.
Dipeptide vinyl sultams: synthesis via the Wittig-Horner reaction and activity against papain, falcipain-2 and Plasmodium falciparum
Bioorg. Med. Chem. Lett.
16
4115-4119
2006
Carica papaya
Theppakorn, T.; Kanasawud, P.; Halling, P.J.
Activity of immobilized papain dehydrated by n-propanol in low-water media
Biotechnol. Lett.
26
133-136
2004
Carica papaya
Lei, H.; Wang, W.; Chen, L.; Li, X.; Yi, B.; Deng, L.
The preparation and catalytically active characterization of papain immobilized on magnetic composite microspheres
Enzyme Microb. Technol.
35
15-21
2004
Carica papaya
-
Konno, K.; Hirayama, C.; Nakamura, M.; Tateishi, K.; Tamura, Y.; Hattori, M.; Kohno, K.
Papain protects papaya tress from herbivorous insects: role of cysteine proteases in latex
Plant J.
37
370-374
2004
Carica papaya
Alphey, M.S.; Hunter, W.N.
High-resolution complex of papain with remnants of a cysteine protease inhibitor derived from Trypanosoma brucei
Acta Crystallogr. Sect. F
F62
504-508
2006
Carica papaya
Gul, S.; Hussain, S.; Thomas, M.P.; Resmini, M.; Verma, C.S.; Thomas, E.W.; Brocklehurst, K.
Generation of nucleophilic character in the Cys25/His159 ion pair of papain involves Trp177 but not Asp158
Biochemistry
47
2025-2035
2008
Carica papaya
Narai-Kanayama, A.; Koshino, H.; Aso, K.
Mass spectrometric and kinetic studies on slow progression of papain-catalyzed polymerization of L-glutamic acid diethyl ester
Biochim. Biophys. Acta
1780
881-891
2008
Carica papaya
Naeem, A.; Fatima, S.; Khan, R.H.
Characterization of partially folded intermediates of papain in presence of cationic, anionic, and nonionic detergents at low pH
Biopolymers
83
1-10
2006
Carica papaya
Theodorou, L.G.; Bieth, J.G.; Papamichael, E.M.
The catalytic mode of cysteine proteinases of papain (C1) family
Biores. Technol.
98
1931-1939
2007
Carica papaya
Haquette, P.; Salmain, M.; Svedlung, K.; Martel, A.; Rudolf, B.; Zakrzewski, J.; Cordier, S.; Roisnel, T.; Fosse, C.; Jaouen, G.
Cysteine-specific, covalent anchoring of transition organometallic complexes to the protein papain from Carica papaya
ChemBioChem
8
224-231
2007
Carica papaya
Martinez, M.; Diaz-Mendoza, M.; Carrillo, L.; Diaz, I.
Carboxy terminal extended phytocystatins are bifunctional inhibitors of papain and legumain cysteine proteinases
FEBS Lett.
581
2914-2918
2007
Carica papaya
Sathish, H.A.; Kumar, P.R.; Prakash, V.
Mechanism of solvent induced thermal stabilization of papain
Int. J. Biol. Macromol.
41
383-390
2007
Carica papaya
Hatori, Y.; Majima, E.; Tsuda, T.; Toyoshima, C.
Domain organization and movements in heavy metal ion pumps: papain digestion of CopA, a Cu+-transporting ATPase
J. Biol. Chem.
282
25213-25221
2007
Carica papaya
Sangeetha, K.; Abraham, T.E.
Chemical modification of papain for use in alkaline medium
J. Mol. Catal. B
38
171-177
2006
Carica papaya
-
Li, G.; Vaidya, A.; Viswanathan, K.; Cui, J.; Xie, W.; Gao, W.; Gross, R.A.
Rapid regioselective oligomerization of L-glutamic acid diethyl ester catalyzed by papain
Macromolecules
39
7915-7921
2006
Carica papaya
-
Grabovac, V.; Schmitz, T.; Foeger, F.; Bernkop-Schnuerch, A.
Papain: an effective permeation enhancer for orally administered low molecular weight heparin
Pharm. Res.
24
1001-1006
2007
Carica papaya
Shabab, M.; Kulkarni, M.J.; Khan, M.I.
Study of papain-cystatin interaction by intensity fading MALDI-TOF-MS
Protein J.
27
7-12
2008
Carica papaya
Lang, A.; Hatscher, C.; Kuhl, P.
Papain-catalyzed synthesis of Z-L-aminoacyl-antipyrine amides from Z-protected amino acid esters and 4-aminoantipyrine
Tetrahedron Lett.
48
3371-3374
2007
Carica papaya (P00784)
-
Cornell, H.J.; Doherty, W.; Stelmasiak, T.
Papaya latex enzymes capable of detoxification of gliadin
Amino Acids
38
155-165
2009
Carica papaya
Diaz-Mochon, J.J.; Planonth, S.; Bradley, M.
From 10,000 to 1: Selective synthesis and enzymatic evaluation of fluorescence resonance energy transfer peptides as specific substrates for chymopapain
Anal. Biochem.
384
101-105
2009
Carica papaya
Xue, Y.; Nie, H.; Zhu, L.; Li, S.; Zhang, H.
Immobilization of Modified Papain with Anhydride Groups on Activated Cotton Fabric
Appl. Biochem. Biotechnol.
160
109-121
2009
Carica papaya, Carica papaya (P00784)
Su, S.N.; Nie, H.L.; Zhu, L.M.; Chen, T.X.
Optimization of adsorption conditions of papain on dye affinity membrane using response surface methodology
Biores. Technol.
100
2336-2340
2009
Carica papaya
Redzynia, I.; Ljunggren, A.; Bujacz, A.; Abrahamson, M.; Jaskolski, M.; Bujacz, G.
Crystal structure of the parasite inhibitor chagasin in complex with papain allows identification of structural requirements for broad reactivity and specificity determinants for target proteases
FEBS J.
276
793-806
2009
Carica papaya (P00784)
Choudhury, D.; Roy, S.; Chakrabarti, C.; Biswas, S.; Dattagupta, J.K.
Production and recovery of recombinant propapain with high yield
Phytochemistry
70
465-472
2009
Carica papaya (P00784)
Homaei, A.A.; Sajedi, R.H.; Sariri, R.; Seyfzadeh, S.; Stevanato, R.
Cysteine enhances activity and stability of immobilized papain
Amino Acids
38
937-942
2010
Carica papaya
Chen, C.X.; Jiang, B.; Branford-White, C.; Zhu, L.M.
Enantioselective reductive amination of alpha-keto acids by papain-based semisynthetic enzyme
Biochemistry (Moscow)
74
36-40
2009
Carica papaya
Chen, T.X.; Nie, H.L.; Li, S.B.; Branford-White, C.; Su, S.N.; Zhu, L.M.
Comparison: adsorption of papain using immobilized dye ligands on affinity membranes
Colloids Surf. B Biointerfaces
72
25-31
2009
Carica papaya
Zhang, Y.; Shi, G.; Zhao, F.
Hydrolysis of casein catalyzed by papain in n-propanol/NaCl two-phase system
Enzyme Microb. Technol.
46
438-443
2010
Carica papaya
Li, S.; Tang, Y.
Accurate determination of internalization for target binding antibody using papain digestion and flow cytometry
Hybridoma
29
133-139
2010
Carica papaya
Andrade, L.B.; Oliveira, A.S.; Ribeiro, J.K.; Kiyota, S.; Vasconcelos, I.M.; de Oliveira, J.T.; de Sales, M.P.
Effects of a novel pathogenesis-related class 10 (PR-10) protein from Crotalaria pallida roots with papain inhibitory activity against root-knot nematode Meloidogyne incognita
J. Agric. Food Chem.
58
4145-4152
2010
Carica papaya
Kempson, I.M.; Barnes, T.J.; Prestidge, C.A.
Use of TOF-SIMS to study adsorption and loading behavior of methylene blue and papain in a nano-porous silicon layer
J. Am. Soc. Mass Spectrom.
21
254-260
2010
Carica papaya
da Silva, C.R.; Oliveira, M.B.; Motta, E.S.; de Almeida, G.S.; Varanda, L.L.; de Padula, M.; Leitao, A.C.; Caldeira-de-Araujo, A.
Genotoxic and cytotoxic safety evaluation of papain (Carica papaya L.) using in vitro assays
J. Biomed. Biotechnol.
2010
197898
2010
Carica papaya
Szabo, A.; Kotorman, M.; Laczko, I.; Simon, L.
Influence of carbohydrates on stability of papain in aqueous tetrahydrofuran mixture
J. Chem. Technol. Biotechnol.
84
133-138
2009
Carica papaya
-
Jeong, J.; Hur, W.
Even-numbered peptides from a papain hydrolysate of silk fibroin
J. Chromatogr.
878
836-840
2010
Carica papaya
Mehta, S.K.; Bhawna, S.K.; Ram, G.
Behavior of papain in mixed micelles of anionic-cationic surfactants having similar tails and dissimilar head groups
J. Colloid Interface Sci.
344
105-111
2010
Carica papaya
Rudolf, B.; Salmain, M.; Martel, A.; Palusiak, M.; Zakrzewski, J.
eta(1)-N-succinimidato complexes of iron, molybdenum and tungsten as reversible inhibitors of papain
J. Inorg. Biochem.
103
1162-1168
2009
Carica papaya
Hyono, A.; Gaboriaud, F.; Mazda, T.; Takata, Y.; Ohshima, H.; Duval, J.F.
Impacts of papain and neuraminidase enzyme treatment on electrohydrodynamics and IgG-mediated agglutination of type A red blood cells
Langmuir
25
10873-10885
2009
Carica papaya
Panicker, S.; Borgia, J.; Fhied, C.; Mikecz, K.; Oegema, T.R.
Oral glucosamine modulates the response of the liver and lymphocytes of the mesenteric lymph nodes in a papain-induced model of joint damage and repair
Osteoarthritis Cartilage
17
1014-1021
2009
Carica papaya
Choudhury, D.; Biswas, S.; Roy, S.; Dattagupta, J.K.
Improving thermostability of papain through structure-based protein engineering
Protein Eng. Des. Sel.
23
457-467
2010
Carica papaya
Zhao, Y.; Gutshall, L.; Jiang, H.; Baker, A.; Beil, E.; Obmolova, G.; Carton, J.; Taudte, S.; Amegadzie, B.
Two routes for production and purification of Fab fragments in biopharmaceutical discovery research: Papain digestion of mAb and transient expression in mammalian cells
Protein Expr. Purif.
67
182-189
2009
Carica papaya
Oliveira, A.S.; Migliolo, L.; Aquino, R.O.; Ribeiro, J.K.; Macedo, L.L.; Bemquerer, M.P.; Santos, E.A.; Kiyota, S.; de Sales, M.P.
Two Kunitz-type inhibitors with activity against trypsin and papain from Pithecellobium dumosum seeds: purification, characterization, and activity towards pest insect digestive enzyme
Protein Pept. Lett.
16
1526-1532
2009
Carica papaya
Shokhen, M.; Khazanov, N.; Albeck, A.
Challenging a paradigm: Theoretical calculations of the protonation state of the Cys25-His159 catalytic diad in free papain
Proteins Struct. Funct. Bioinform.
77
916-926
2009
Carica papaya
Zulli, G.; Lopes, P.; Velasco, M.; Alcantara, M.; Rogero, S.; Lugao, A.; Mathor, M.
Influence of gamma radiation onto polymeric matrix with papain
Radiat. Phys. Chem.
79
286-288
2010
Carica papaya
-
Hu, W.; Guan, Z.; Deng, X.; He, Y.H.
Enzyme catalytic promiscuity: The papain-catalyzed Knoevenagel reaction
Biochimie
94
656-661
2012
Carica papaya
de Beer, R.J.; Zarzycka, B.; Amatdjais-Groenen, H.I.; Jans, S.C.; Nuijens, T.; Quaedflieg, P.J.; van Delft, F.L.; Nabuurs, S.B.; Rutjes, F.P.
Papain-catalyzed peptide bond formation: enzyme-specific activation with guanidinophenyl esters
ChemBioChem
12
2201-2207
2011
Carica papaya
Chu, M.H.; Liu, K.L.; Wu, H.Y.; Yeh, K.W.; Cheng, Y.S.
Crystal structure of tarocystatin-papain complex: implications for the inhibition property of group-2 phytocystatins
Planta
234
243-254
2011
Carica papaya (P00784)
Li, M.; Su, E.; You, P.; Gong, X.; Sun, M.; Xu, D.; Wei, D.
Purification and in situ immobilization of papain with aqueous two-phase system
PLoS ONE
5
e15168
2010
Carica papaya
Llerena-Suster, C.; Jose, C.; Collins, S.; Briand, L.; Morcelle, S.
Investigation of the structure and proteolytic activity of papain inaqueous miscible organic media
Process Biochem.
47
47-56
2012
Carica papaya
-
Shokhen, M.; Khazanov, N.; Albeck, A.
The mechanism of papain inhibition by peptidyl aldehydes
Proteins
79
975-985
2011
Carica papaya (P00784)
Homaei, A.; Barkheh, H.; Sariri, R.; Stevanato, R.
Immobilized papain on gold nanorods as heterogeneous biocatalysts
Amino Acids
46
1649-1657
2014
Carica papaya
Kim, C.J.; Lee, D.I.; Lee, C.H.; Ahn, I.S.
A dityrosine-based substrate for a protease assay: application for the selective assessment of papain and chymopapain activity
Anal. Chim. Acta
723
101-107
2012
Carica papaya
Uygun, D.A.; Akduman, B.; Uygun, M.; Akgoel, S.; Denizli, A.
Purification of papain using reactive green 5 attached supermacroporous monolithic cryogel
Appl. Biochem. Biotechnol.
167
552-563
2012
Carica papaya
Fan, Y.; Yan, J.; Zhang, S.; Li, J.; Chen, D.; Duan, P.
Fluorescence spectroscopic analysis of the interaction of papain with ionic liquids
Appl. Biochem. Biotechnol.
168
592-603
2012
Carica papaya
Chalabi, M.; Khademi, F.; Yarani, R.; Mostafaie, A.
Proteolytic activities of kiwifruit actinidin (Actinidia deliciosa cv. Hayward) on different fibrous and globular proteins: a comparative study of actinidin with papain
Appl. Biochem. Biotechnol.
172
4025-4037
2014
Carica papaya
Wei, D.; Huang, X.; Liu, J.; Tang, M.; Zhan, C.G.
Reaction pathway and free energy profile for papain-catalyzed hydrolysis of N-acetyl-Phe-Gly 4-nitroanilide
Biochemistry
52
5145-5154
2013
Carica papaya
Rudakova, A.S.; Rudakov, S.V.; Kakhovskaya, I.A.; Shutov, A.D.
11S Storage globulin from pumpkin seeds: regularities of proteolysis by papain
Biochemistry
79
820-825
2014
Carica papaya
Mohr, T.; Desser, L.
Plant proteolytic enzyme papain abrogates angiogenic activation of human umbilical vein endothelial cells (HUVEC) in vitro
BMC Complement. Altern. Med.
13
231
2013
Carica papaya
Esti, M.; Benucci, I.; Lombardelli, C.; Liburdi, K.; Garzillo, A.
Papain from papaya (Carica papaya L.) fruit and latex: Preliminary characterization in alcoholic-acidic buffer for wine application
Food Bioprod. Process.
91
595-598
2013
Carica papaya
Alpay, P.; Uygun, D.
Usage of immobilized papain for enzymatic hydrolysis of proteins
J. Mol. Catal. B
111
56-63
2015
Carica papaya
-
Richau, K.H.; Kaschani, F.; Verdoes, M.; Pansuriya, T.C.; Niessen, S.; Stueber, K.; Colby, T.; Overkleeft, H.S.; Bogyo, M.; Van der Hoorn, R.A.
Subclassification and biochemical analysis of plant papain-like cysteine proteases displays subfamily-specific characteristics
Plant Physiol.
158
1583-1599
2012
Carica papaya
Milosevic, J.; Jankovic, B.; Prodanovic, R.; Polovic, N.
Comparative stability of ficin and papain in acidic conditions and the presence of ethanol
Amino Acids
51
829-838
2019
Carica papaya (P00784)
Mugita, N.; Nambu, T.; Takahashi, K.; Wang, P.L.; Komasa, Y.
Proteases, actinidin, papain and trypsin reduce oral biofilm on the tongue in elderly subjects and in vitro
Arch. Oral Biol.
82
233-240
2017
Carica papaya (P00784)
Lachmanova, S.; Kolivoska, V.; Pospisil, L.; Fanelli, N.; Hromadova, M.
Adsorption of papain on solid substrates of different hydrophobicity
Biointerphases
11
031003
2016
Carica papaya (P00784)
Liu, J.; Sharma, A.; Niewiara, M.; Singh, R.; Ming, R.; Yu, Q.
Papain-like cysteine proteases in Carica papaya lineage-specific gene duplication and expansion
BMC Genomics
19
26
2018
Carica papaya (P00784), Carica papaya
Pan, A.D.; Zeng, H.Y.; Foua, G.B.; Alain, C.; Li, Y.Q.
Enzymolysis of chitosan by papain and its kinetics
Carbohydr. Polym.
135
199-206
2016
Carica papaya (P00784)
Roy, S.; Biswas, S.
Asp72 of pro-peptide is an important pH sensor in the zymogen activation process of papain A structural and mechanistic insight
Curr. Sci.
114
2356-2362
2018
Carica papaya (P00784)
-
Homaei, A.; Samari, F.
Investigation of activity and stability of papain by adsorption on multi-wall carbon nanotubes
Int. J. Biol. Macromol.
105
1630-1635
2017
Carica papaya (P00784)
Homaei, A.
Enhanced activity and stability of papain immobilized on CNBr-activated sepharose
Int. J. Biol. Macromol.
75
373-377
2015
Carica papaya (P00784)
Leichner, C.; Menzel, C.; Laffleur, F.; Bernkop-Schnuerch, A.
Development and in vitro characterization of a papain loaded mucolytic self-emulsifying drug delivery system (SEDDS)
Int. J. Pharm.
530
346-353
2017
Carica papaya (P00784)
Barekat, S.; Soltanizadeh, N.
Application of high-intensity ultrasonic radiation coupled with papain treatment to modify functional properties of beef Longissimus lumborum
J. Food Sci. Technol.
56
224-232
2019
Carica papaya (P00784)
Feng, L.; Cao, Y.; Xu, D.; Zhang, D.; Huang, Z.
Influence of chitosan-sodium alginate pretreated with ultrasound on the enzyme activity, viscosity and structure of papain
J. Sci. Food Agric.
97
1561-1566
2017
Carica papaya (P00784)
Liu, X.; Zeng, H.; Liao, M.; Claude Alain Gohi, B.; Feng, B.
Determination of the kinetics and influence of the mercury ion on papain catalytic activity
RSC Adv.
5
68906-68913
2015
Carica papaya (P00784)
-
Zhang, B.; Li, P.; Zhang, H.; Fan, L.; Wang, H.; Li, X.; Tian, L.; Ali, N.; Ali, Z.; Zhang, Q.
Papain/Zn3(PO4)2 hybrid nanoflower Preparation, characterization and its enhanced catalytic activity as an immobilized enzyme
RSC Adv.
6
46702-46710
2016
Carica papaya (P00784)
-
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