3.4.22.2: papain
This is an abbreviated version!
For detailed information about papain, go to the full flat file.
Word Map on EC 3.4.22.2
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3.4.22.2
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cathepsins
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proteinases
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chymotrypsin
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pepsin
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cystatins
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bromelain
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igg
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hydrolysates
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cartilage
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immunoglobulin
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ficin
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pronase
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proteoglycans
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erythrocyte
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glycosaminoglycans
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alpha-chymotrypsin
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elastase
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neuraminidase
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chondroitin
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alcalase
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subtilisin
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latex
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thermolysin
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carica
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allergen
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articular
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agglutination
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collagenase
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emphysema
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plasmin
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kininogens
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fab\'2
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anti-d
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intra-articular
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bacteriocins
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pineapple
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legumains
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l-like
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pancreatin
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meromyosin
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dermatan
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emphysematous
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chondroitinase
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antiglobulin
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nutrition
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actin-activated
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medicine
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food industry
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enzyme-treated
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industry
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alloantibody
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subfragment-1
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analysis
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synthesis
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carlsberg
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biotechnology
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procathepsins
- 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
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articular
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agglutination
- collagenase
- emphysema
- plasmin
- kininogens
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fab\'2
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anti-d
-
intra-articular
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bacteriocins
- pineapple
- legumains
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l-like
- pancreatin
- meromyosin
- dermatan
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emphysematous
- chondroitinase
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antiglobulin
- nutrition
-
actin-activated
- medicine
- food industry
-
enzyme-treated
- industry
-
alloantibody
-
subfragment-1
- analysis
- synthesis
-
carlsberg
- biotechnology
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procathepsins
Reaction
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
Adolph's Meat Tenderizer, arbuz, CpXCP5, EC 3.4.4.10, enzeco papain, papain, papain-like cysteine protease, papain-like protease, papaine, papaya peptidase I, papaya proteinase 1, Papaya proteinase I, papayotin, PLCP, PLpro, PPI, summetrin, velardon
ECTree
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Inhibitors
Inhibitors on EC 3.4.22.2 - papain
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(2-[(S,R)-2-oxo-4-phenylazetidin-1-yl]acetyl)-L-phenylalanine methyl ester
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weak inhibitor, irreversible
(2-[(S,R)-2-oxo-4-phenylazetidin-1-yl]acetyl)-L-Val benzyl ester
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weak inhibitor, irreversible
(eta5-C5H5)Fe(CO)3 eta1-N-succinimidato
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metallocarbonyl complex, reversible inhibitor
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(eta5-C5H5)Mo(CO)3 eta1-N-succinimidato
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metallocarbonyl complex, reversible inhibitor
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(eta5-C5H5)W(CO)3 eta1-N-succinimidato
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metallocarbonyl complex, reversible inhibitor
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(S)-1-[(S)-N-(tert-butyloxycarbonyl)alanyl]-4-oxoazetidine-2-carboxylic acid
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weak, irreversible inactivation
(S,R)-1-[(S)-N-(tert-butyloxycarbonyl)alanyl]-4-phenylazetidin-2-one
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weak inhibitor, irreversible
1,1-dicyano-2-(4,5-dimethoxy-2-nitrophenyl)-ethene
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irreversible, photosensitive inhibitor
1-(4,5-dimethoxy-2-nitrophenyl)-2-nitroethene
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irreversible, photosensitive inhibitor
acetyl-Phe-Gly-S-nitrosopenicillamine
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inactivation of papain by S-nitrosothiols is due to a direct attack of the highly reactive thiolate Cys25 in the enzyme active site on the sulfur of S-nitrosothiols to form a mixed disulfide between the inactivator and papain
barley cystatin protease inhibitor
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inhibited by various cystatin vatiants, HvCPI-1, HvCPI-2, HvCPI-3, HvCPI-4, HvCPI-5, HvCPI-6
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benzyl-(S)-1-[(S)-N-(tert-butyloxycarbonyl)alanyl]-4-oxoazetidine-2-carboxylate
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weak, irreversible inactivation
benzyl-(S)-2-(benzyloxycarbonyl)azetidin-1-acetate
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weak, irreversible inactivation
benzyloxycarbonyl-Phe-Ala-glyoxal
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competitive, 13C-NMR study of the inhibition
chitosan
the Haldane kinetic model adequately describes the dynamic behavior of the chitosan enzymolysis by papain. When the initial chitosan concentration is above 8.0 g/l, the papain is overloaded and exhibits significant inhibition
CNWAAGYNCGGGS-NH2
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synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
CNWTLGGYKCGGGS-NH2
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synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
Co2+
5 mM, 46% loss of activity (soluble enzyme), 30% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
CpPRI
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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
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Cu2+
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residual activity in the presence of 20 mM: 0% free papain, 20% immobilized papain
CWEWGGWHCGGSS-OH
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synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
CWSMMGFQCGGGS-NH2
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weak inhibition, synthetic cyclic peptide, cyclization through intramolecular disulfide bonding
dimethyl sulfoxide
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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
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number of papain active sites decreases with increase of inhibitor concentration
endopin 2
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highly effective inhibition, cross-class inhibition of papain and elastase. Localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells
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ethanol
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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
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weak inhibitor, irreversible
Fe2+
5 mM, 44% loss of activity (soluble enzyme), 32% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
glucose-2S-nitroso-N-acetyl-penicillamine
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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
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weak inhibition, synthetic cyclic peptide, cyclization head-to-tail
Hg2+
papain activity increases to a maximum of 111.03% (non-competitive type activation) at a concentration of 0.000001x01mol/l Hg2+, but is almost completely deactivated at concentrations above 0.0001 mol/lx01Hg2+. The inhibition of Hg2+ on papain is a competitive and uncompetitive mixed type inhibition
Kunitz type trypsin inhibitor
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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
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methanol
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number of papain active sites decreases with increase of inhibitor concentration
Ni2+
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residual activity in the presence of 20 mM: 0% free papain, 16% immobilized papain
oryzacastatin
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and fragments. The NH2-terminal 21 rsidues including Gly5 and the COOH-terminal 11 residues of the inhibitor are not essential for inhibition
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papain inhibitors
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A1, A2, A3, B2 and C from seeds of Vigna unguiculata subsp. cylindrica
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PdKl-3.1
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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
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PdKl-3.2
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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
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S-nitroso-N-acetyl-DL-penicillamine
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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
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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
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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
tarocystatin
the N-terminal cystatin domain (residues 1-98) of tarocystatin has inhibitory ability against papain
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Urea
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the reversible unfolding/refolding process of the PLpro in the presence of urea is investigated. The zinc-binding domain of the enzyme starts to unfold at urea concentration below 0.35 M and reaches a first plateau at 1-3.5 M. At this stage, the palm and thumb core domains remain well folded but totally inactive
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residual activity in the presence of 20 mM: 13% free papain, 38% immobilized papain
Ba2+
5 mM, 24% loss of activity (soluble enzyme), 9% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
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residual activity in the presence of 20 mM: 10% free papain, 48% immobilized papain
Ca2+
5 mM, 22% loss of activity (soluble enzyme), 6% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
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residual activity in the presence of 20 mM: 20% free papain, 57% immobilized papain
Mg2+
5 mM, 19% loss of activity (soluble enzyme), 4% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
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residual activity in the presence of 20 mM: 0% free papain, 18% immobilized papain
Mn2+
5 mM, 44% loss of activity (soluble enzyme), 31% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
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residual activity in the presence of 20 mM: 0% free papain, 16% immobilized papain
Zn2+
5 mM, 51% loss of activity (soluble enzyme), 45% loss of activity (enzyme immobilized by covalent attachment on Sepharose 6B activated by using cyanogen bromide)
loosely packed papain prosegment displays inhibitory activity but can also function as activator for the mature enzyme, overview
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additional information
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no inhibition by synthetic cyclic peptide CTSPRLHPCGGGS-NH2, interaction anaylsis of enzyme with diverse synthetic peptides in a phage display assay, overview
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additional information
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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
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additional information
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several buffers decrease the activity of the n-propanol dehydrated, immobilized enzyme in low-water tert-butanol medium, overview
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additional information
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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))
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additional information
immobilization of papain by covalent attachment on Sepharose 6B activated by using cyanogen bromide brings about resistance against the inhibitory effects of various bivalent metal ions with respect to papain
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