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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
preferential cleavage: Gly-/-, in proteins and small molecule substrates
Synonyms
glycyl endopeptidase, papaya proteinase iv, chymopapain m, papaya peptidase b, glycine endopeptidase, papaya proteinase 4,
more
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glycine endopeptidase
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Proteinase, glycine-specific
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additional information
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the enzyme belongs to the C1A peptidase family
Chymopapain M
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Glycyl endopeptidase
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Papaya peptidase B
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Papaya proteinase 4
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Papaya proteinase 4
UniProt
Papaya proteinase IV
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PPIV
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preferential cleavage: Gly-/-, in proteins and small molecule substrates
preferential cleavage: Gly-/-, in proteins and small molecule substrates
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preferential cleavage: Gly-/-, in proteins and small molecule substrates
specific for Gly at posotion P1 due to an exchange conserved residues Gly23 to Glu and Gly65 to Arg, 2 free thiol functions of cysteinyl residues are essential for the catalytic competence of the enzyme
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hydrolysis of peptide bond
hydrolysis of peptide bond
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hydrolysis of peptide bond
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aggrecan + H2O
?
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azocasein + H2O
trichloroacetic acid-soluble peptides from azocasein
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10% of the activity of papain
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benzyloxycarbonyl-Gly-Leu-NH + H2O
L-leucine amide + N-benzyloxycarbonyl-glycine
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-
-
?
benzyloxycarbonyl-Gly-Phe-NH + H2O
L-phenylalanine amide + N-benzyloxycarbonyl-glycine
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-
?
benzyloxycarbonyl-Gly-Tyr-NH + H2O
L-tyrosine amide + N-benzyloxycarbonyl-glycine
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-
?
benzyloxycarbonyl-Gly-Tyr-Oet + H2O
L-tyrosine ethyl ester + N-benzyloxycarbonyl-glycine
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?
casein + H2O
trichloroacetic acid-soluble peptides derived from casein
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10% of the activity of papain
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Gly-4-nitroanilide + H2O
glycine + 4-nitroaniline
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-
-
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?
Hemoglobin + H2O
Trichloroacetic acid-soluble peptides from haemoglobin
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hide powder azure + H2O
?
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N-Acetyl-L-Phe-Gly 4-nitroanilide + H2O
?
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N-Benzyloxycarbonyl-Gly 4-nitrophenyl ester + H2O
?
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tert-Butyloxycarbonyl-Ala-Ala-Ala 4-methylcoumarin 7-amide + H2O
?
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tert-Butyloxycarbonyl-Ala-Ala-Gly 4-methylcoumarin 7-amide + H2O
?
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tert-Butyloxycarbonyl-Ala-Ala-Gly 4-nitroanilide + H2O
?
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tert-butyloxycarbonyl-Ala-Ala-Gly-p-nitroanilide + H2O
tert-butyloxycarbonyl-Ala-Ala-Gly + p-nitroaniline
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?
Trypsin + H2O
Hydrolyzed trypsin
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16 cleavage points of which 13 are glycyl bonds
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additional information
?
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Chicken cystatin + H2O
?
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Chicken cystatin + H2O
?
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?
Human cystatin C + H2O
?
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Human cystatin C + H2O
?
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?
protein + H2O
peptides
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?
protein + H2O
peptides
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?
additional information
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synthetic substrates of other papaya proteinases
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additional information
?
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absolute specificity for substrates with glycine at the P1 position (structural origin of the unusual specificity)
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additional information
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not: cystatin A
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additional information
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the recombinant proregion of the enzyme can inhibit the cysteine protease of larvae of the Colorado beetle, Leptinotarsa decemlineata, analoguesly to specific inhibitor oryzacystatin I, inhibitory effect is affected by temperature
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?
additional information
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the enzyme is useful for the plant defense system
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additional information
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substrate specificity with preference for glycyl residues, structure-function relationship, overview, hydrolyzes glycine esters but not Bz-Arg-4-nitroanilide
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additional information
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glycyl endopeptidase fails to hydrolyse DL-benzyl-Arg-p-nitroanilide
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additional information
?
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protein + H2O
peptides
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?
protein + H2O
peptides
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?
additional information
?
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the recombinant proregion of the enzyme can inhibit the cysteine protease of larvae of the Colorado beetle, Leptinotarsa decemlineata, analoguesly to specific inhibitor oryzacystatin I, inhibitory effect is affected by temperature
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?
additional information
?
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the enzyme is useful for the plant defense system
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Alpha-macroglobulin
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L-3-carboxy-2,3-epoxypropionylleucylamido(4-guanidino)butane
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Peptide aldehydes
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despite the presence of bulky sidechains in P1
Pro-peptide
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the enzyme is inhibited by its own pro region after cleavage, also pro-peptide of other C1 peptidase family enzymes can be inhibitory
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iodoacetamide
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low rate of inactivation
iodoacetamide
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slow inactivation
iodoacetate
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low rate of inactivation
iodoacetate
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slow inactivation
Peptidyl diazomethanes
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containing glycine in P1 and a hydrophobic side-chain in P2
Peptidyl diazomethanes
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Peptidyl diazomethanes
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dependent on the substrate
additional information
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human cystatin A; human cystatin C; not: chicken cystatin
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additional information
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not: chicken cystatin
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additional information
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cystatin family of cysteine proteinase inhibitors
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additional information
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not: chicken cystatin (structural origin of the lack of inhibition)
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additional information
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no inhibition by most cystatins
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additional information
not inhibited by cystatin
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additional information
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the enzyme depends on a thiolate ion for activity
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0.08
tert-butyloxycarbonyl-Ala-Ala-Ala 4-methylcoumarin 7-amide
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0.16
tert-butyloxycarbonyl-Ala-Ala-Gly 4-methylcoumarin 7-amide
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5.2
tert-butyloxycarbonyl-Ala-Ala-Gly 4-nitroanilide
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0.08
tert-butyloxycarbonyl-Ala-Ala-Ala 4-methylcoumarin 7-amide
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5
tert-butyloxycarbonyl-Ala-Ala-Gly 4-methylcoumarin 7-amide
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22
tert-butyloxycarbonyl-Ala-Ala-Gly 4-nitroanilide
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0.0000034
papapya cystatin
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0.00086
Pro-peptide
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7 - 7.5
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tert-butyloxycarbonyl-Ala-Ala-Gly 4-nitroanilide
additional information
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pI: 10.6-10.7
7
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azocasein
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3 - 9.5
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3.0: 15% of maximal activity, 9.5: about 75% of maximal activity, tert-butyloxycarbonyl-Ala-Ala-Gly 4-nitroanilide
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30143 , 30144 , 30145 , 30146 , 30147 , 30148 , 30149 , 30150 , 30151 , 30152 , 30153 , 30154 , 30155 , 651248 , 652619 , 667431 , 668767 -
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brenda
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UniProt
brenda
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brenda
from commercial chymopapain
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brenda
var. Zhonghuang
UniProt
brenda
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brenda
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unripe
brenda
green fruit skin has the highest enzyme content, ripening decreases the enzyme level
brenda
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brenda
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brenda
Papaya latex is usually harvested from fruit skin of green papaya fruits by mechanical wounding
brenda
additional information
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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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brenda
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latex
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brenda
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brenda
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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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PAPA4_CARPA
348
0
39024
Swiss-Prot
L1L9H3_THEEQ
494
1
57140
TrEMBL
A0A396JA97_MEDTR
293
1
32793
TrEMBL
A0A396IKU7_MEDTR
197
0
22552
TrEMBL
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23310
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Carica papaya, calculation from amino acid sequence
24000
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Carica papaya, sedimentation analysis, meniscus depletion method
additional information
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three-dimensional structure
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additional information
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three-dimensional structure comparison to other latex peptidase
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proteolytic modification
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the enzyme is synthesized as preproenzyme
additional information
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enzyme is synthesized as inactive proenzyme, and rapidly converted to the active from within 2 min after wounding of the plant
no glycoprotein
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no site of potential glycosylation detected
no glycoprotein
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mature enzyme
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G27E
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site-directed mutagenesis, high reduced activity with substrate having an Arg at P1 position
G73R
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site-directed mutagenesis, high reduced activity with substrate having an Arg at P1 position, decreased affinity for cystatin C
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additional information
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the enzyme undergoes a conformational transition at low pH and 37°C, that instantaneously and irreversibly converts the native form into molten globules, which are unstable and rapidly degraded by pepsin
667431
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37
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recombinant proregion, 60 min, stable
additional information
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factors effecting thermostability
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ammonium sulfate precipitation
different methods, overview
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glycyl endopeptidase from papaya latex is partitioned using aqueous two-phase (10% PEG 6000- 10% (NH4)2SO4) in combination with NH4(SO4)2 precipitation.The partially purified glycyl endopeptidase shows the potential in production of antioxidative gelatin hydrolysates. The enzyme fraction contain lower odorous compounds in papaya latex. The gelatin hydrolysate produced using the selected fraction have negligible odorous compounds
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native enzyme from latex by ion exchange and adsorption chromatography, and gel filtration
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several ligands possible for affinity chromatography are presented, fractionation on hydrophobic and cation-exchange supports, overview
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expression of the pro-region of papaya proteinase IV in Escherichia coli
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expression of the proregion of the enzyme in Escherichia coli
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gene CpXCP7, genotyping using the peptidase_C1 domain, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis
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biotechnology
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plant protease proregions have a potential as regulators of cysteine proteinases in biotechnological systems and to target proteases of pests
nutrition
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the enzyme needs to be protected from acid denaturation and proteolysis in the gut after oral administration to be effective as cysteine protease
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Polgar, L.
Isolation of highly active papaya peptidases A and B from commercial chymopapain
Biochim. Biophys. Acta
658
262-269
1981
Carica papaya
brenda
Ritonja, A.; Buttle, D.J.; Rawlings, N.D.; Turk, V.; Barrett, A.J.
Papaya proteinase IV amino acid sequence
FEBS Lett.
258
109-112
1989
Carica papaya
brenda
Buttle, D.J.; Ritonja, A.; Pearl, L.H.; Turk, V.; Barrett, A.J.
Selective cleavage of glycyl bonds by papaya proteinase IV
FEBS Lett.
260
195-197
1990
Carica papaya
brenda
Buttle, D.J.; Ritonja, A.; Dando, P.M.; Abrahamson, M.; Shaw, E.N.; Wikstrom, P.; Turk, V.; Barrett, A.J.
Interactions of papaya proteinase IV with inhibitors
FEBS Lett.
262
58-60
1990
Carica papaya
brenda
Buttle, D.J.
Glycyl endopeptidase
Methods Enzymol.
244
539-555
1994
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
Dekeyser, P.M.; Buttle, D.J.; Devreese, B.; van Beeumen, J.; Demeester, J.; Lauwers, A.
Kinetic constants for the hydrolysis of aggrecan by the papaya proteinases and their relevance for chemonucleolysis
Arch. Biochem. Biophys.
320
375-379
1995
Carica papaya
brenda
Buttle, D.J.; Kembhavi, A.A.; Sharp, S.L.; Shute, R.E.; Rich, D.H.; Barrett, A.J.
Affinity purification of the novel cysteine proteinase papaya proteinase IV, and papain from papaya latex
Biochem. J.
261
469-476
1989
Carica papaya
brenda
O'Hara, B.P.; Hemmings, A.M.; Buttle, D.J.; Pearl, L.H.
Crystal structure of glycyl endopeptidase from Carica papaya: a cysteine endopeptidase of unusual substrate specificity
Biochemistry
34
13190-13195
1995
Carica papaya
brenda
Thomas, M.P.; Verma, C.; Boyd, S.M.; Brocklehurst, K.
The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin
Biochem. J.
306
39-46
1995
Carica papaya
brenda
Topham, C.M.; Overington, J.; Thomas, M.; Kowlessur, D.; Thomas, E.W.; Brocklehurst, K.
Three-dimensional structure and thiol reactivity characteristics of chymopapain M (papaya proteinase IV)
Biochem. Soc. Trans.
18
934-935
1990
Carica papaya
brenda
Thomas, M.P.; Topham, C.M.; Kowlessur, D.; Mellor, G.W.; Thomas, E.W.; Whitford, D.; Brocklehurst, K.
Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain
Biochem. J.
300
805-820
1994
Carica papaya
brenda
Goodenough, P.E.; Owen, J.
Chromatographic and electrophoretic analyses of papaya proteinases
Phytochemistry
26
75-79
1987
Carica papaya
-
brenda
Taylor, M.A.J.; Briggs, G.S.; Baker, K.C.; Cummings, N.J.; Pratt, K.A.; Freeman, R.B.; Goodenough, P.W.
Expression of the pro-regions of papain and papaya proteinase IV in Escherichia coli and their inhibition of mature cysteine proteinases
Biochem. Soc. Trans.
23
80S
1995
Carica papaya
brenda
Visal, S.; Taylor, M.A.; Michaud, D.
The proregion of papaya proteinase IV inhibits Colorado potato beetle digestive cysteine proteinases
FEBS Lett.
434
401-405
1998
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
Buttle, D.J.
Glycyl endopeptidase
Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D., Woessner, J.F., eds)
2
1132-1134
2004
Carica papaya
-
brenda
Chaiwut, P.; Kanasawud, P.; Halling, P.J.
Solid-to-solid peptide synthesis by glycyl endopeptidase
Enzyme Microb. Technol.
40
954-960
2007
Carica papaya (P05994)
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brenda
Karnjanapratum, S.; Benjakul, S.
Glycyl endopeptidase from papaya latex: partial purification and use for production of fish gelatin hydrolysate
Food Chem.
165
403-411
2014
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, Carica papaya (P05994)
brenda
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