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Information on EC 3.4.22.25 - glycyl endopeptidase
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3.4.22.25 glycyl endopeptidaseSpecify your search results
Word Map
- 3.4.22.25
- proteinases
- latex
- cystatins
- caricain
- cathepsins
-
subsite
-
3.4.22.6
-
herbivorous
-
chemonucleolysis
- beta-trypsin
-
cation-exchange
- pro-regions
- biotechnology
- nutrition
The enzyme appears in viruses and cellular organisms
Synonyms
Chymopapain, Chymopapain M, CpXCP7, glycine endopeptidase, Glycyl endopeptidase, More, Papaya peptidase B, Papaya proteinase 4, Papaya proteinase IV, PPIV, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Chymopapain M
Glycyl endopeptidase
Papaya peptidase B
Papaya proteinase 4
Papaya proteinase IV
PPIV
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
preferential cleavage: Gly-/-, in proteins and small molecule substrates
-
-
-
-
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
149719-24-4
-
92228-52-9
-
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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
azocasein + H2O
trichloroacetic acid-soluble peptides from azocasein
-
10% of the activity of papain
-
?
benzyloxycarbonyl-Gly-Leu-NH + H2O
L-leucine amide + N-benzyloxycarbonyl-glycine
-
-
-
?
benzyloxycarbonyl-Gly-Phe-NH + H2O
L-phenylalanine amide + N-benzyloxycarbonyl-glycine
-
-
-
?
benzyloxycarbonyl-Gly-Tyr-NH + H2O
L-tyrosine amide + N-benzyloxycarbonyl-glycine
-
-
-
?
benzyloxycarbonyl-Gly-Tyr-Oet + H2O
L-tyrosine ethyl ester + N-benzyloxycarbonyl-glycine
-
-
-
?
casein + H2O
trichloroacetic acid-soluble peptides derived from casein
-
10% of the activity of papain
-
?
Hemoglobin + H2O
Trichloroacetic acid-soluble peptides from haemoglobin
-
-
-
?
tert-Butyloxycarbonyl-Ala-Ala-Gly 4-methylcoumarin 7-amide + H2O
?
-
-
-
-
?
tert-butyloxycarbonyl-Ala-Ala-Gly-p-nitroanilide + H2O
tert-butyloxycarbonyl-Ala-Ala-Gly + p-nitroaniline
-
-
-
?
Trypsin + H2O
Hydrolyzed trypsin
-
16 cleavage points of which 13 are glycyl bonds
-
?
additional information
?
-
-
synthetic substrates of other papaya proteinases
-
-
?
additional information
?
-
-
absolute specificity for substrates with glycine at the P1 position (structural origin of the unusual specificity)
-
-
?
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme is useful for the plant defense system
-
-
?
additional information
?
-
-
substrate specificity with preference for glycyl residues, structure-function relationship, overview, hydrolyzes glycine esters but not Bz-Arg-4-nitroanilide
-
-
?
additional information
?
-
glycyl endopeptidase fails to hydrolyse DL-benzyl-Arg-p-nitroanilide
-
-
?
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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
additional information
?
-
-
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
-
?
additional information
?
-
-
the enzyme is useful for the plant defense system
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Pro-peptide
-
the enzyme is inhibited by its own pro region after cleavage, also pro-peptide of other C1 peptidase family enzymes can be inhibitory
-
Peptidyl diazomethanes
-
containing glycine in P1 and a hydrophobic side-chain in P2
additional information
-
human cystatin A; human cystatin C; not: chicken cystatin
-
additional information
-
not: chicken cystatin (structural origin of the lack of inhibition)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma
Electrophoretic analysis of the "cross-class" interaction between novel inhibitory serpin, squamous cell carcinoma antigen-1 and cysteine proteinases.
Carcinoma, Squamous Cell
Electrophoretic analysis of the "cross-class" interaction between novel inhibitory serpin, squamous cell carcinoma antigen-1 and cysteine proteinases.
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9.5
-
3.0: 15% of maximal activity, 9.5: about 75% of maximal activity, tert-butyloxycarbonyl-Ala-Ala-Gly 4-nitroanilide
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
green fruit skin has the highest enzyme content, ripening decreases the enzyme level
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). PAPA4_CARPA
348
0
39024
Swiss-Prot
Secretory Pathway (Reliability: 1)
L1L9H3_THEEQ
494
1
57140
TrEMBL
other Location (Reliability: 5)
A0A396IKU7_MEDTR
197
0
22552
TrEMBL
Mitochondrion (Reliability: 5)
A0A396JA97_MEDTR
293
1
32793
TrEMBL
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
three-dimensional structure comparison to other latex peptidase
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
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
G27E
-
site-directed mutagenesis, high reduced activity with substrate having an Arg at P1 position
G73R
-
site-directed mutagenesis, high reduced activity with substrate having an Arg at P1 position, decreased affinity for cystatin C
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
native enzyme from latex by ion exchange and adsorption chromatography, and gel filtration
-
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
gene CpXCP7, genotyping using the peptidase_C1 domain, phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
plant protease proregions have a potential as regulators of cysteine proteinases in biotechnological systems and to target proteases of pests
nutrition
-
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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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
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)
-
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 (P05994), Carica papaya
brenda
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