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Information on EC 3.4.22.6 - chymopapain and Organism(s) Carica papaya and UniProt Accession P14080
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3.4.22.6 chymopapainSpecify your search results
Word Map
- 3.4.22.6
-
chemonucleolysis
- disc
-
lumbar
-
herniated
-
intervertebral
-
intradiscal
- pulposus
- sciatica
- proteinases
- anaphylaxis
-
percutaneous
- proteoglycans
- latex
-
anaphylactic
- spine
-
nucleolysis
-
radicular
-
microdiscectomy
-
immunomagnetic
-
decompress
-
myelography
-
hernia
-
prick
- keratan
- bromelain
- chondroitinase
- caricain
-
diskectomy
- fibrosus
- ficin
-
dura
-
prolapsed
-
discogenic
-
anulus
-
low-back
- actinidin
-
myelogram
- nutrition
- medicine
-
3.4.22.2
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
Synonyms
chymopapain, chymopapain a, chymopapain b, chymopapain isoform ii, chymopapain isoform iv, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chymopapain
chymopapain A
-
-
-
-
chymopapain B
-
-
-
-
Chymopapain S
-
-
-
-
papaya proteinase II
-
-
-
-
PPII
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CAS REGISTRY NUMBER
COMMENTARY
9001-09-6
-
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
2,4-dichlorocyclohexan-1-one + cyclohexanone
?
yield: 43%, 80:20 anti/syn, ee (anti): 81%
-
-
?
2,6-dichlorocyclohexan-1-one + cyclohexanone
?
yield: 39%, 99:01 anti/syn, ee (anti): 58%
-
-
?
2-chlorocyclohexan-1-one + cyclohexanone
?
yield: 30%, 86:14 anti/syn, ee (anti): 79%
-
-
?
2-nitrocyclohexan-1-one + cyclohexanone
?
yield: 24%, 87:13 anti/syn, ee (anti): 82%
-
-
?
3-chlorocyclohexan-1-one + cyclohexanone
?
yield: 32%, 65:35 anti/syn, ee (anti): 93%
-
-
?
3-nitrocyclohexan-1-one + cyclohexanone
?
yield: 41%, 87:13 anti/syn, ee (anti): 86%
-
-
?
4-bromocyclohexan-1-one + cyclohexanone
?
yield: 29%, 81:19 anti/syn, ee (anti): 84%
-
-
?
4-chlorocyclohexan-1-one + cyclohexanone
?
yield: 47%, 69:31 anti/syn, ee (anti): 75%
-
-
?
4-cyanocyclohexan-1-one + cyclohexanone
?
yield: 60%, 72:28 anti/syn, ee (anti): 76%
-
-
?
4-methylcyclohexan-1-one + cyclohexanone
?
yield: 23%, 63:37 anti/syn, ee (anti): 96%
-
-
?
4-nitrocyclohexan-1-one + acetaldehyde
?
yield: 12%, ee (anti): 14%
-
-
?
4-nitrocyclohexan-1-one + cycloheptanone
?
yield: 19%, 47:53 anti/syn, ee (anti): 26%
-
-
?
4-nitrocyclohexan-1-one + cyclohexanone
?
yield: 69%, 63:37 anti/syn, ee (anti): 78%
-
-
?
4-nitrocyclohexan-1-one + cyclopentanone
?
yield: 73%, 56:44 anti/syn, ee (anti): 52%
-
-
?
furan-2-carbaldehyde + cyclohexanone
?
yield: 16%, 63:37 anti/syn, ee (anti): 61%
-
-
?
N,N-diBoc-dityrosine-(isoniacid)2 + H2O
N,N-diBoc-dityrosine + 2 isoniacid
-
-
-
?
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide + H2O
benzyloxycarbonyl-Phe-Arg-4-methylcoumarin 7-amide
-
-
-
-
?
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
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N5-(5-carboxyfluorescein))-NH2 + H2O
methyl red-Abu-Ser-Ala-Pro-Val-Lys + Ala-Lys(N5-(5-carboxyfluorescein))-NH2
-
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-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + p-nitroaniline
-
-
-
-
?
N-alpha-benzoylphenylalanine-arginine-4-methylcoumarin-7-amide + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly p-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + p-nitrophenol
-
-
-
-
?
succinyl-Phe-Arg-p-nitroanilide + H2O
succinyl-Phe-Arg + p-nitroaniline
-
mechanism of action
-
-
?
4-cyanobenzaldehyde + cyclohexanone
4-[hydroxy(2-oxocyclohexyl)methyl]benzonitrile
catalytic activity and stereoselectivity of chymopapainare influenced by different media. Best catalytic activity and moderate stereoselectivity in DMSO (yield: 50%, anti/syn ratio 55:45, ee(anti): 40%), best enantioselectivity in CH2Cl2 (yield: 18%, anti/syn ratio: 61:39, ee(anti): 79%)
-
-
?
4-cyanobenzaldehyde + cyclohexanone
4-[hydroxy(2-oxocyclohexyl)methyl]benzonitrile
solvent: water/MeCN. The water content greatly affects the activity and selectivity of chymopapain for the aldol reaction. The best enantioselectivity and diastereoselectivity at the water content of 0.12 (water/MeCN, v/v), which give the product in a yield of 28% with 73:27 (anti/syn ratio) and 77% ee (for anti isomer). Best enzyme activity at the water content of 0.15, which give a yield of 32% with lower selectivity
-
-
?
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-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2 + H2O
methyl red-Abu-Ala-Pro-Val-Lys + Lys(N5-(5-carboxyfluorescein))-NH2
-
pH 6.2 or pH 7.4, 10 min, 37°C
-
-
?
N-benzoyl-Arg-4-nitroanilide + H2O
N-benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
N-benzoyl-Arg-4-nitroanilide + H2O
N-benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
additional information
?
-
-
the abnormal catalytic site environment of chymopapain A may have consequences for the acylation step of the catalytic act, does not pertub the conformation of the bound acyl group at the acyl-enzyme-intermediate stage of catalysis
-
-
?
additional information
?
-
-
mass spectroscopy studies show unequivocally the specificity of chymopapain toward Ala, Pro, Val and Lys for positions P4 to P1 while not presenting high specificity for residues in position P1
-
-
?
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
2,4-dichlorocyclohexan-1-one + cyclohexanone
?
yield: 43%, 80:20 anti/syn, ee (anti): 81%
-
-
?
2,6-dichlorocyclohexan-1-one + cyclohexanone
?
yield: 39%, 99:01 anti/syn, ee (anti): 58%
-
-
?
2-chlorocyclohexan-1-one + cyclohexanone
?
yield: 30%, 86:14 anti/syn, ee (anti): 79%
-
-
?
2-nitrocyclohexan-1-one + cyclohexanone
?
yield: 24%, 87:13 anti/syn, ee (anti): 82%
-
-
?
3-chlorocyclohexan-1-one + cyclohexanone
?
yield: 32%, 65:35 anti/syn, ee (anti): 93%
-
-
?
3-nitrocyclohexan-1-one + cyclohexanone
?
yield: 41%, 87:13 anti/syn, ee (anti): 86%
-
-
?
4-bromocyclohexan-1-one + cyclohexanone
?
yield: 29%, 81:19 anti/syn, ee (anti): 84%
-
-
?
4-chlorocyclohexan-1-one + cyclohexanone
?
yield: 47%, 69:31 anti/syn, ee (anti): 75%
-
-
?
4-cyanocyclohexan-1-one + cyclohexanone
?
yield: 60%, 72:28 anti/syn, ee (anti): 76%
-
-
?
4-methylcyclohexan-1-one + cyclohexanone
?
yield: 23%, 63:37 anti/syn, ee (anti): 96%
-
-
?
4-nitrocyclohexan-1-one + acetaldehyde
?
yield: 12%, ee (anti): 14%
-
-
?
4-nitrocyclohexan-1-one + cycloheptanone
?
yield: 19%, 47:53 anti/syn, ee (anti): 26%
-
-
?
4-nitrocyclohexan-1-one + cyclohexanone
?
yield: 69%, 63:37 anti/syn, ee (anti): 78%
-
-
?
4-nitrocyclohexan-1-one + cyclopentanone
?
yield: 73%, 56:44 anti/syn, ee (anti): 52%
-
-
?
furan-2-carbaldehyde + cyclohexanone
?
yield: 16%, 63:37 anti/syn, ee (anti): 61%
-
-
?
additional information
?
-
-
mass spectroscopy studies show unequivocally the specificity of chymopapain toward Ala, Pro, Val and Lys for positions P4 to P1 while not presenting high specificity for residues in position P1
-
-
?
4-cyanobenzaldehyde + cyclohexanone
4-[hydroxy(2-oxocyclohexyl)methyl]benzonitrile
catalytic activity and stereoselectivity of chymopapainare influenced by different media. Best catalytic activity and moderate stereoselectivity in DMSO (yield: 50%, anti/syn ratio 55:45, ee(anti): 40%), best enantioselectivity in CH2Cl2 (yield: 18%, anti/syn ratio: 61:39, ee(anti): 79%)
-
-
?
4-cyanobenzaldehyde + cyclohexanone
4-[hydroxy(2-oxocyclohexyl)methyl]benzonitrile
solvent: water/MeCN. The water content greatly affects the activity and selectivity of chymopapain for the aldol reaction. The best enantioselectivity and diastereoselectivity at the water content of 0.12 (water/MeCN, v/v), which give the product in a yield of 28% with 73:27 (anti/syn ratio) and 77% ee (for anti isomer). Best enzyme activity at the water content of 0.15, which give a yield of 32% with lower selectivity
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
crystals from potato tubers are predominantly composed of a proteinase inhibitor with a MW of 80000 Da, that inhibits chymopapain
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thioglycolic acid
-
maximal activity in presence of various reducing compounds, e.g. Cys, 2,3-dimercaptopropanol, thioglycolic acid, glutathione
2,3-Dimercaptopropanol
-
maximal activity in presence of various reducing compounds, e.g. Cys, 2,3-dimercaptopropanol, thioglycolic acid, glutathione
Cys
-
maximal activity in presence of various reducing compounds, e.g. Cys, 2,3-dimercaptopropanol, thioglycolic acid, glutathione
glutathione
-
maximal activity in presence various reducing compounds, e.g. Cys, 2,3-dimercaptopropanol, thioglycolic acid, glutathione
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0502
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
pH 7.4
0.0502
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline
0.0506
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
pH 6.2
0.0506
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
0.023
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
pH 6.2
0.023
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
0.026
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
pH 7.4
0.026
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
246
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
590
methyl red-Abu-Ala-Pro-Val-Lys-Lys(N5-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline
133
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
360
methyl red-Abu-Ser-Ala-Pro-Val-Lys-Ala-Lys(N6-(5-carboxyfluorescein))-NH2
-
at pH 7.4, in 100 mM phosphate-buffered saline
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.91
assay at. Chymopapain shows the best activity and enantioselectivity in the presence of phosphate buffer (pH 4.91, buffer/MeCN:0.12, v/v), which give the product in yield of 45% with 72:28 (anti/syn ratio) and 78% ee (for anti isomer)
7.2
enzyme is dissolved in phosphate buffer and used with a suspension of lysosomes in 0.154 mol/l sodium chloride
additional information
pH value of the reaction medium plays a significant role in maintaining the stability and catalytic activity of the enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
best diastereoselectivity and enantioselectivity is reached at 30°C, which give a yield of 27% with 76:24 (anti/syn ratio) and 78% ee (for anti isomer)
37
additional information
temperature is an important factor affecting the enzyme stability, selectivity and reaction rate
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
-
latex from ripe and unripe fruit. Repeated wounding results in either accumulation or activation of enzyme as well as papain, caricain and more cysteine proteases
additional information
Papaya latex is usually harvested from fruit skin of green papaya fruits by mechanical wounding
-
-
30247, 30257, 81552, 81559, 81565, 81567, 81568, 81569, 81571, 652619, 667431, 678400, 678751, 680560, 707651
-
repeated wounding results in either, accumulation or activation (or both of them) of chymopapain
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
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). PAPA2_CARPA
352
0
39415
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
fraction is 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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the enzyme is synthesized as inactive precursor that converts into mature enzyme within 2 min after wounding the plant when the latex is abruptly expelled
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1
-
at low pH, the enzyme undergoes a conformational transition that instantaneously converts their native form into molten globule that are quite unstable and rapidly degraded by pepsin. The denatured state of these proteinase which results from acid treatment is completely irreversible
667431
1.5
-
protein unfolds following biphasic kinetics. Two different effects of electrolyte concentration on unfolding reaction are observed. At low ionic strength, the ionic atmosphere causes an increase in reaction rates, regardless of the type of ions being present. This effect is attributed to a general electrostatic screening of charge-charge interactions in the macromolecule. At high ionic strength, each electrolyte exerts a distinctly different effect: both rate constants are largely increased by guanidinium-HCl but slightly by LiCl. Na2SO4 decreases the value of both unfolding rates
678400
2 - 3
-
enzyme undergoes conformational transition that instantaneously converts the native form into a molten globule state and is completely irreversible
667431
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
irreversible thermal denaturation according to a first order reaction in which the macromolecule is globally unfolded
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during purification, the thiol function of the Cys residues are protected either as mixed disulfides with cysteamine or 2-thiopyridone or as S-sulfenylthiosulfate derivative or after blocking with PCMB
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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
supports: phenyl-Hg+ CH3COO- and glutathione-S-S-(2-pyridyl), further purification through the S-thiol poly(ethylene glycol) derivatization technique
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene CpXCP8, genotyping using the peptidase_C1 domain, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
down regulated protein in papaya sticky diseased latex
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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
medicine
-
significantly more nucleus can be removed from a disc using a bilateral rather than a unilateral approach. A unilateral approach using rongeurs alone leads to removal of only about one-third of the nucleus. Rongeurs, followed by chymopapain, lead to removal of significantly more nucleus than when rongeurs are used alone. The most effective method is a bilateral approach using rongeurs followed by chymopapain where about three-quarters of the nucleus can be removed. This approach can create sufficient space for the implant insertion. A brush, which can be inserted through a trocar, assists in the removal of strands of nucleus that are loosened by chymopapain. Experiments are carried out on sheep spines since they are increasingly being used as models for human spines
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brocklehurst, K.; Baines, B.S.; Salih, E.; Hatzoulis, C.
Chymopapain S is chymopapain A
Biochem. J.
221
553-554
1984
Carica papaya
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
Robinson, G.W.
Isolation and characterization of papaya peptidase A from commercial chymopapain
Biochemistry
14
3695-3700
1975
Carica papaya
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
Solis-Mendiola, S.; Zubillaga-Luna, R.; Rojo-Dominguez, A.; Hernandez-Arana, A.
Structural similarity of chymopapain forms as indicated by circular dichroism
Biochem. J.
257
183-186
1989
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
Solis-Mendiola, S.; Gutierrez-Gonzales, L.H.; Arroyo-Reyna, A.; Padilla-Zuniga, J.; Rojo-Dominguez, A.; Hernandez-Arana, A.
pH Dependence of the activation parameters for chymopapain unfolding: influence of ion pairs on the kinetic stability of proteins
Biochim. Biophys. Acta
1388
363-372
1998
Carica papaya
Azarkan, M.; Maes, D.; Bouckaert, J.; Dao Thi, M.H.; Wyns, L.; Looze, Y.
Thiol pegylation facilitates purification of chymopapain leading to diffraction studies at 1.4 A resolution
J. Chromatogr. A
749
69-72
1996
Carica papaya
-
Buttle, D.J.; Barrett, A.J.
Chymopapain. Chromatographic purification and immunological characterization
Biochem. J.
223
81-88
1984
Carica papaya
Rodis, P.; Hoff, J.E.
Naturally occurring protein crystals in the potato. Inhibitor of papain, chymopapain, and ficin
Plant Physiol.
74
907-911
1984
Carica papaya
Khan, I.U.; Polgar, L.
Purification and characterization of a novel proteinase, chymopapain S
Biochim. Biophys. Acta
760
350-356
1983
Carica papaya
-
Kunimitsu, D.K.; Yasunobu, K.T.
Chymopapain B
Methods Enzymol.
19
244-252
1970
Carica papaya
-
Kunimitsu, D.K.; Yasunobu, K.T.
Chymopapain. IV. The chromatographic fractionation of partially purified chymopapain and the characterization of crystalline chymopapain B
Biochim. Biophys. Acta
139
405-417
1967
Carica papaya
Ebata, M.; Yasunobu, K.T.
Chymopapain. I. Isolation, crystallization, and preliminary characterization
J. Biol. Chem.
237
1086-1094
1962
Carica papaya
Vincentelli, J.; Bouckaert, J.; Jacquet, A.; Paul, C.; Thi, M.H.S.; Poortmans, F.; Wyns, L.; Looze, Y.
Purification of chymopapain as a single fully active cysteine-proteinase led to reexamination of its catalytic properties and to crystallization
Int. J. Bio-Chromatogr.
1
209-226
1995
Carica papaya
-
Maes, D.; Bouckaert, J.; Poortmans, F.; Wyns, L.; Looze, Y.
Structure of chymopapain at 1.7 A resolution
Biochemistry
35
16292-16298
1996
Carica papaya
Walreavens, V.; Jaziri, M.; van Bleeumen, J.; Schnek, A.G.; Kleinschmidt, T.; Looze, Y.
Isolation and preliminary characterization of the cysteine-proteinases from the latex of Carica candamarcensis Hook
Biol. Chem. Hoppe-Seyler
374
501-506
1993
Carica papaya, Vasconcellea cundinamarcensis, Vasconcellea cundinamarcensis Hook
Jaquet, A.; Kleinschmidt, T.; Schnek, A.G.; Looze, Y.; Braunitzer, G.
The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain
Biol. Chem. Hoppe-Seyler
370
425-434
1989
Carica papaya
Buttle, D.J.; Dando, P.M.; Coe, P.F.; Sharp, S.L.; Shepherd, S.T.; Barrett, A.J.
The preparation of fully active chymopapain free of contaminating proteinases
Biol. Chem. Hoppe-Seyler
371
1083-1088
1990
Carica papaya
Bjrk, I.; Ylinenjrvi, K.
Interaction between chicken cystatin and the cysteine proteinases actinidin, chymopapain A, and ficin
Biochemistry
29
1770-1776
1990
Carica papaya
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
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
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
Lopez-Arenas, L.; Solis-Mendiola, S.; Padilla-Zuniga, J.; Hernandez-Arana, A.
Hofmeister effects in protein unfolding kinetics: estimation of changes in surface area upon formation of the transition state
Biochim. Biophys. Acta
1764
1260-1267
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
Dang, L.; Wardlaw, D.; Hukins, D.W.
Removal of nucleus pulposus from the intervertebral disc - the use of chymopapain enhances mechanical removal with rongeurs: a laboratory study
BMC Musculoskelet. Disord.
8
122
2007
Carica papaya
Fatima, S.; Khan, R.H.
Effect of polyethylene glycols on the function and structure of thiol proteases
J. Biochem.
142
65-72
2007
Carica papaya
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 (P14080)
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
Chen, W.H.; Liu, H.Y.; Lo, W.C.; Wu, S.C.; Chi, C.H.; Chang, H.Y.; Hsiao, S.H.; Wu, C.H.; Chiu, W.T.; Chen, B.J.; Deng, W.P.
Intervertebral disc regeneration in an ex vivo culture system using mesenchymal stem cells and platelet-rich plasma
Biomaterials
30
5523-5533
2009
Carica papaya
Guo, J.; Yang, L.; Liu, X.; Zhang, H.; Qian, B.; Zhang, D.
Applicability of the chymopapain gene used as endogenous reference gene for transgenic huanong no. 1 papaya detection
J. Agric. Food Chem.
57
6502-6509
2009
Carica papaya (Q5Q047), Carica papaya
He, Y.; Li, H.; Chen, Y.; Xue, Y.; Yuan, Y.; Guan, Z.
Chymopapain-catalyzed direct asymmetric aldol reaction
Adv. Synth. Catal.
354
712-719
2012
Carica papaya (P14080)
-
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 (P14080)
Rodrigues, S.P.; Ventura, J.A.; Aguilar, C.; Nakayasu, E.S.; Choi, H.; Sobreira, T.J.; Nohara, L.L.; Wermelinger, L.S.; Almeida, I.C.; Zingali, R.B.; Fernandes, P.M.
Label-free quantitative proteomics reveals differentially regulated proteins in the latex of sticky diseased Carica papaya L. plants
J. Proteomics
75
3191-3198
2012
Carica papaya (P14080), Carica papaya (Q9SMH9), Carica papaya (Q9SMI0), Carica papaya (Q9SMI2)
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