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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, 
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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
-
-
-
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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
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hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
mechanism, Asp158 is involved in catalysis
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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
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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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