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Information on EC 3.4.22.30 - Caricain
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3.4.22.30 CaricainSpecify your search results
Word Map
- 3.4.22.30
- proteinases
- latex
- actinidin
- ficin
-
catalytic-site
-
glycyl
-
papain-like
-
2,2\'-dipyridyl
-
active-centre
- drug development
- food industry
- nutrition
The expected taxonomic range for this enzyme is: Carica papaya
Reaction Schemes
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Synonyms
caricain, papaya peptidase a, papaya proteinase omega, ppiii, proteinase omega, procaricain, papaya proteinase iii, papaya peptidase ii, papaya proteinase 3, ppomega, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
caricain
Chymopapain S
-
-
-
-
Papaya peptidase A
-
-
-
-
Papaya peptidase II
-
-
-
-
Papaya proteinase 3
-
-
-
-
Papaya proteinase A
-
-
-
-
Papaya proteinase III
Papaya proteinase OMEGA
PPIII
-
-
-
-
PpOmega
-
-
-
-
Proteinase omega
-
-
-
-
Proteinase, papaya A
-
-
-
-
Proteinase, papaya, III
-
-
-
-
additional information
Papaya proteinase III
-
-
-
-
Papaya proteinase OMEGA
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
-
-
-
-
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
mechanism
-
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
mechanism
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Asp158 is not involved in ionization and catalytic competence
-
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
mechanism, Asp158 is involved in catalysis
-
hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
residue E50 is part of the electrostatic switch required for catalytic activity, mechanism, possible role of D158
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
39307-22-7
-
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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
alpha-N-benzoyl-L-arginine 4-nitroanilide + H2O
alpha-N-benzoyl-L-arginine + 4-nitroaniline
-
-
-
?
N-acetyl-Phe-Gly methylthionoester + H2O
?
-
synthetic chromogenic substrate, reaction mechanism, computer modeling of intermediate formation
-
?
N-benzoyl-L-arginine ethyl ester + H2O
N-benzoyl-L-arginine + ethanol
-
isoform caricain II, low activity
-
-
?
N-tosyl-L-Arg methyl ester + H2O
N-tosyl-L-Arg + methanol
-
less active than papain
-
-
?
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroaniline
-
-
-
?
pyr-Glu-Phe-Leu-4-nitroanilide + H2O
pyr-Glu-Phe-Leu + 4-nitroaniline
-
-
?
casein + H2O
?
-
isoform caricain II, twofold activity on casein compared to caricain
-
-
?
Gliadin + H2O
?
-
a rat liver lysosome assay is used to monitor the extent of detoxification of a gliadin digest by caricain. Pre-incubating the gliadin digest for different durations with caricain allows the kinetics of the detoxification process to be studied. A significant degree of protection (80%) of the lysosomes is achieved with 1.7% w/w of caricain on substrate after incubation for 2 h at 37 °C. The detoxification follows first-order kinetics with a rate constant of 0.00017/sec
-
-
?
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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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide
-
competitive to succinyl-albumin
Gly-Gly(O-benzyl)Tyr-Arg
-
competitive, affinity is dependent on ionic strength and always lower than that of papain
Succinyl-albumin
-
competitive to benzyloxycarbonyl-Phe-Arg 4-methylcoumarin 7-amide
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
i.e. E-64, irreversible, active site-directed
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiol group
-
enzyme contains 1 thiol group per molecule, this thiol group is essential for catalytic activity
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hypersensitivity
Comparative modelling of major house dust mite allergen Der p I: structure validation using an extended environmental amino acid propensity table.
Hypersensitivity
Immunoglobulin E antibodies to papaya proteinases and their relevance to chemonucleolysis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kcat/Km ratio (pH-dependence of)
-
additional information
additional information
-
kinetics of the reaction with substrate N-acetyl-Phe-Gly methylthionoester
-
additional information
additional information
-
kinetics of wild-type and D158N mutant
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pH-dependence of kcat/Km ratio
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
additional information
6.8
enzyme is dissolved in phosphate buffer and used with a suspension of lysosomes in 0.154 mol/l sodium chloride
additional information
-
papaya peptidase A is an enzyme of extreme basicity and has a higher isoelectric point than any of the other enzymes in papaya latex
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
additional information
additional information
-
determination of minimum energy conformation, interaction of ionized and un-ionized side chains of Asp158 and their microenvironment
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
green fruit skin has the highest enzyme content, ripening decreases the enzyme level
brenda
additional information
-
-
30142, 30147, 30154, 30247, 30248, 30250, 30252, 30253, 30255, 30256, 30257, 30258, 30259, 30260, 30261, 30262, 652619, 695532
brenda
-
latex from ripe and unripe fruit. Repeated wounding results in either accumulation or activation of enzyme as well as papain, chymopapain and more cysteine proteases
brenda
Papaya latex is usually harvested from fruit skin of green papaya fruits by mechanical wounding
brenda
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
brenda
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
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
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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). PAPA3_CARPA
348
0
38788
Swiss-Prot
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18800
-
x * 18800, purified from enzyme solution. Protein lacks the N-terminal 41 residues of enzyme, disulfide bond C22-C63 is opened
24000
40000
procaricain, fractions are estimated from plots of Kav against molecular weight using dextran blue, human gamma-globulin, bovine serum albumin and trypsin inhibitor as standards, mass spectrometric analysis of trypsin-digested fractions from chromatography are carried out by liquid chromatography/electrospray quadrupole time-of-flight mass spectrometry in positive mode
additional information
additional information
-
three-dimensional structure deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 18800, purified from enzyme solution. Protein lacks the N-terminal 41 residues of enzyme, disulfide bond C22-C63 is opened
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme is synthesized as inactive proenzyme, and rapidly converted to the active from within 2 min after wounding of the plant
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D158N
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 3
-
enzyme undergoes conformational transition that instantaneously converts the native form into a molten globule state and is completely irreversible
667431
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
denaturation occurs as a non two-state process, via an intermediate structure, thermodynamic characteristics
additional information
-
thermal denaturing kinetics, autolysis during denaturation is prevented by irreversible blockage of the active-site thiol with idoacetamide
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, preparation of the mercury derivative of fully active papaya peptidase A, 50fold molar excess of DTT, 30 days stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme is semi-purified with from latex crude extracts by ion exchange chromatography on a CM Sephadex column C-50 and gel filtration
recombinant wild-type and mutant enzymes from Escherichia coli, to homogeneity
to homogeneity, several ligands possible for affinity chromatography are presented, fractionation on hydrophobic and cation-exchange supports, overview
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
genotyping using the peptidase_C1 domain, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis
overexpression of wild-type and mutant enzymes in Escherichia coli BL21(DE3)
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from inclusion bodies after overexpression in scherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
caricain would be suitable for enzyme therapy in gluten intolerance and appears to have synergistic action with porcine intestinal extracts, potential for enzyme therapy in coeliac disease
nutrition
-
at low pH, enzyme undergoes conformational transition leading to instability and rapid degradation by pepsin. To be effective in gut after oral administration, enzyme needs to be protected against acid denaturation and degradation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Polgar, L.
Isolation of highly active papaya peptidases A and B from commercial chymopapain
Biochim. Biophys. Acta
658
262-269
1981
Carica papaya
brenda
Sumner, I.G.; Harris, G.W.; Taylor, M.A.J.; Pickersgill, R.W.; Owen, A.J.; Goodenough, P.W.
Factors effecting the thermostability of cysteine proteinases from Carica papaya
Eur. J. Biochem.
214
129-134
1993
Carica papaya
brenda
Goodenough, P.E.; Owen, J.
Chromatographic and electrophoretic analyses of papaya proteinases
Phytochemistry
26
75-79
1987
Carica papaya
-
brenda
Brocklehurst, K.; Baines, B.S.; Salih, E.; Hatzoulis, C.
Chymopapain S is chymopapain A
Biochem. J.
221
553-554
1984
Carica papaya
brenda
Polgar, L.
Problems of classification of papaya latex proteinases
Biochem. J.
221
555-556
1984
Carica papaya
brenda
Brocklehurst, K.; Salih, E.; McKee, R.; Smith, H.
Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase omega
Biochem. J.
228
525-527
1985
Carica papaya
brenda
Barrett, A.J.; Buttle, D.J.
Names and numbers of papaya proteinases
Biochem. J.
228
527
1985
Carica papaya
brenda
Dubois, T.; Kleinschmidt, T.; Schnek, A.G.; Looze, Y.; Braunitzer, G.
The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega
Biol. Chem. Hoppe-Seyler
369
741-754
1988
Carica papaya
brenda
Zucker, S.; Buttle, D.J.; Nicklin, M.J.H.; Barrett, A.J.
The proteolytic activities of chymopapain, papain, and papaya proteinase III
Biochim. Biophys. Acta
828
196-204
1985
Carica papaya
brenda
Baines, B.S.; Brocklehurst, K.
Characterization of papaya peptidase A as a cysteine proteinase of Carica papaya L. with active-centre properties that differ from those of papain by using 2,2-dipyridyl disulphide and 4-chloro-7-nitrobenzofurazan as reactivity probes. Use of two-protonic-state electrophiles in the identification of catalytic-site thiol groups
Biochem. J.
205
205-211
1982
Carica papaya
brenda
Robinson, G.W.
Isolation and characterization of papaya peptidase A from commercial chymopapain
Biochemistry
14
3695-3700
1975
Carica papaya
brenda
Goodenough, P.W.; Owen, J.
Papaya proteinases separated by novel means have been used to generate monoclonal antibodies
Biochem. Soc. Trans.
15
264-265
1987
Carica papaya
-
brenda
Baines, B.S.; Brocklehurst, K.; Carey, P.R.; Jarvis, M.; Salih, E.; Storer, A.C.
Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives
Biochem. J.
233
119-129
1986
Carica papaya
brenda
Schack, P.; Kaarsholm, N.C.
Absence in papaya peptidase A catalyzed hydrolyses of a pKa apprx. 4 present in papain-catalyzed hydrolyses
Biochemistry
23
631-635
1984
Carica papaya
-
brenda
Schack, P.; Kaarsholm, N.C.
Subsite differences between the active centres of papaya peptidase A and papain as revealed by affinity chromatography. Purification of papaya peptidase A by ionic-strength-dependent affinity adsorption on an immobilized peptide inhibitor of papain
Biochem. J.
219
727-733
1984
Carica papaya
brenda
Sumner, I.G.; Vaughan, A.; Eisenthal, R.; Pickersgill, R.W.; Owen, A.J.; Goodenough, P.W.
Kinetic analysis of papaya proteinase omega
Biochim. Biophys. Acta
1164
243-251
1993
Carica papaya
brenda
Topham, C.M.; Salih, E.; Frazao, C.; Kowlessur, D.; Overington, J.P.; Thomas, M.; Brocklehurst, S.M.; Patel, M.; Thomas, E.W.; Brocklehurst, K.
Structure-function relationships in the cysteine proteinases actinidin, papain and papaya proteinase omega. Three-dimensional structure of papaya proteinase omega deduced by knowledge-based modelling and active-centre characteristics determined by two-hydronic-state reactivity probe kinetics and kinetics of catalysis
Biochem. J.
280
79-92
1991
Carica papaya
brenda
Kaarsholm, N.C.; Schack, P.
Characterization of papaya peptidase A as an enzyme of extreme basicity
Acta Chem. Scand. B
37
607-611
1983
Carica papaya
brenda
Noble, M.A.; Gul, S.; Verma, C.S.; Brocklehurst, K.
Ionization characteristics and chemical influences of aspartic acid residue 158 of papain and caricain determined by structure-related kinetic and computational techniques: multiple electrostatic modulators of active-centre chemistry
Biochem. J.
351
723-733
2000
Carica papaya
brenda
Reid, J.D.; Hussain, S.; Sreedharan, S.K.; Bailey, T.S.F.; Pinitglang, S.; Thomas, E.W.; Verma, C.S.; Brocklehurst, K.
Variation in aspects of cysteine proteinase catalytic mechanism deduced by spectroscopic observation of dithioester intermediates, kinetic analysis and molecular dynamics simulations
Biochem. J.
357
343-352
2001
Carica papaya
brenda
Pinitglang, S.; Patel, M.; Noble, M.; Sreedharan, S.K.; Verma, C.; Thomas, E.W.; Brocklehurst, K.
Effects of the quality of the P2-S2 hydrophobic contacts on the catalytic activities of papain, caricain and ficin and their generation by electrostatic switches
Biochem. Soc. Trans.
25
88S
1997
Carica papaya
brenda
Noble, M.; Abramson, D.; Verma, C.; Brocklehurst, K.
Evidence that the carboxy groups of Asp158 in papain and caricain have abnormally low pKa values and thus do not contribute the key ionizations with pKa 4 that generate catalytic competence
Biochem. Soc. Trans.
25
90S
1997
Carica papaya
brenda
Khan, A.; Connerton, I.F.; Cummings, N.J.; Hussain, S.; Noble, M.A.; Taylor, M.A.J.; Thomas, E.W.; Verma, C.; Brocklehurst, K.
The kinetically influential ionizations of caricain D158N revealed by using 4,4'-dipyrimidyl disulfide as a reactivity probe
Biochem. Soc. Trans.
26
S172
1998
Carica papaya
brenda
Lopez-Arenas, L.; Solis-Mendiola, S.; Hernandez-Arana, A.
Estimating the degree of expansion in the transition state for protein unfolding: analysis of the pH dependence of the rate constant for caricain denaturation
Biochemistry
38
15936-15943
1999
Carica papaya
brenda
Ikeuchi, Y.; Katerelos, N.A.; Goodenough, P.W.
The enhancing of a cysteine proteinase activity at acidic pH by protein engineering, the role of glutamic 50 in the enzyme mechanism of caricain
FEBS Lett.
437
91-96
1998
Carica papaya (P10056), Carica papaya
brenda
Azarkan, M.; El Moussaoui, A.; van Wuytswinkel, D.; Dehon, G.; Looze, Y.
Fractionation and purification of the enzymes stored in the latex of Carica papaya
J. Chromatogr. B
790
229-238
2003
Carica papaya
brenda
Huet, J.; Looze, Y.; Bartik, K.; Raussens, V.; Wintjens, R.; Boussard, P.
Structural characterization of the papaya cysteine proteinases at low pH
Biochem. Biophys. Res. Commun.
341
620-626
2006
Carica papaya
brenda
Azarkan, M.; Dibiani, R.; Baulard, C.; Baeyens-Volant, D.
Effects of mechanical wounding on Carica papaya cysteine endopeptidases accumulation and activity
Int. J. Biol. Macromol.
38
216-224
2006
Carica papaya
brenda
Liu, W.; Ye, W.; Wang, Z.; Chao, H.; Lian, J.
Preparation and characterization of a truncated caricain lacking 41 residues from the N-terminal
Protein J.
24
243-251
2005
Carica papaya
brenda
Cornell, H.J.; Doherty, W.; Stelmasiak, T.
Papaya latex enzymes capable of detoxification of gliadin
Amino Acids
38
155-165
2009
Carica papaya, Carica papaya (P10056)
brenda
Cornell, H.; Stelmasiak, T.
Caricain: A basis for enzyme therapy for coeliac disease
South Afr. J. Sci.
107
75-79
2011
Carica papaya
-
brenda
Buddrick, O.; Cornell, H.J.; Small, D.M.
Reduction of toxic gliadin content of wholegrain bread by the enzyme caricain
Food Chem.
170
343-347
2015
Carica papaya (P10056), Carica papaya
brenda
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 (P10056), Carica papaya
brenda
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