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EC Tree
The enzyme appears in viruses and cellular organisms
Reaction Schemes
preferential cleavage of peptides with a proline residue at the P2 position
Synonyms
gp-ii, zingibain, ginger protease, zingipain,
more
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cysteine proteinase GP-II
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F50
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GP-II
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preferential cleavage of peptides with a proline residue at the P2 position
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hydrolysis of peptide bond
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acetoacetate decarboxylase + H2O
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bovine casein + H2O
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Bovine serum albumin + H2O
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Collagen + H2O
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Gelatin + H2O
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Lysozyme + H2O
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Myoglobin + H2O
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additional information
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azocasein + H2O
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azocasein + H2O
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azocasein + H2O
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additional information
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enzyme prefers to cleave peptide bonds at which Pro is in the P2 position
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additional information
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enzyme prefers to cleave peptide bonds at which Pro is in the P2 position
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additional information
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enzyme prefers to cleave peptide bonds at which Pro is in the P2 position
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additional information
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enzyme prefers to cleave peptide bonds at which Pro is in the P2 position
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additional information
?
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initial cleavage is at peptide bonds with P2 Pro
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Cu2+
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activates at 1-10 mM
Fe2+
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activates at 1 mM, inhibits at 10 mM
Hg2+
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activates at 1 mM, complete inhibition at 5-10 mM
Mg2+
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activates at 1 mM, inhibits at 10 mM
Mn2+
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activates at 1-10 mM
Zn2+
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activates at 1 mM, inhibits at 10 mM
additional information
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the purified enzyme is highly stable against numerous metal ions
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4-chloromercuribenzoate
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EDTA
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about 60% inhibition at 1-10 mM
Fe2+
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activates at 1 mM, inhibits at 10 mM
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane
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additional information
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no activating or inhibitory, but a stabilizing effect by EDTA, no inhibition by K+ and Na+
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Co2+
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slight inhibition
Cu2+
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complete inhibition
Hg2+
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activates at 1 mM, complete inhibition at 5-10 mM
Hg2+
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complete inhibition
Mg2+
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activates at 1 mM, inhibits at 10 mM
Zn2+
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activates at 1 mM, inhibits at 10 mM
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additional information
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no activating or inhibitory, but a stabilizing effect by EDTA
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SDS
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SDS
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enhances by 27.4% at 0.25 mM
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Diabetes Mellitus, Type 2
Production of a novel wheat gluten hydrolysate containing dipeptidyl peptidase-IV inhibitory tripeptides using ginger protease.
Infections
HSV-1 gB and VZV gp-II crossreactive antibodies in human sera.
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additional information
casein
additional information
casein
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Km value is 0.446 mg/ml, pH 7.0, 40°C
additional information
additional information
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Km and Vmax values are 0.21 mg/ml and 34.48 mg/m/min, respectively, with substrate azocasein
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0.005
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purified native enzyme, substrate bovine casein, pH 7.0, 40°C
27.6
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purified native enzyme, substrate azocasein, pH 7.0, 60°C
3573
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pH not specified in the publication, temperature not specified in the publication
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7
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broad optimum at pH 6.0-7.5
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4 - 8.5
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activity range, profile overview
4.5 - 9.5
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activity range, profile overview
5 - 9.5
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activity range, profile overview
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20 - 80
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activity range, profile overview
25 - 80
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activity range, profile overview
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4.38
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isoelectric focussing
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brenda
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brenda
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SwissProt
brenda
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brenda
from Malaysia
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brenda
var. Bentong, from Malaysia
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brenda
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brenda
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brenda
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brenda
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brenda
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evolution
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the enzyme has sequence similarity with zingipain-1 from Zingiber officinalis
additional information
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the enzyme has cysteine protease activity, but also a significant acetylcholinesterase inhibitor activity exhibiting noncompetitive inhibition of acetylcholinesterase for the hydrolysis of acetylthiocholine iodide with a Ki value of 9.31 mg/ml., overview
physiological function
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zingipain shows antiproliferative activities against fungi, i.e. Fusarium oxysporum, Exserohilum turicicum, and Collectotrichum cassicola, and human malignant cell lines, e.g. Hep-G2 and SW-620, although not against bacterial cells
physiological function
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zingipain shows antiproliferative activities against fungi, i.e. Fusarium oxysporum, Exserohilum turicicum, and Collectotrichum cassicola, and human malignant cell lines, e.g. Hep-G2 and SW-620, although not against bacterial cells
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CPGP1_ZINOF
221
0
24244
Swiss-Prot
other Location (Reliability: 2 )
CPGP2_ZINOF
221
0
23922
Swiss-Prot
other Location (Reliability: 1 )
A0A2P6Q837_ROSCH
202
0
21957
TrEMBL
Secretory Pathway (Reliability: 3 )
A0A2P6SGL9_ROSCH
139
0
14446
TrEMBL
other Location (Reliability: 4 )
A0A2P6RUL4_ROSCH
186
0
19521
TrEMBL
other Location (Reliability: 3 )
A0A396H1A0_MEDTR
210
0
23048
TrEMBL
Mitochondrion (Reliability: 5 )
A0A396J2L5_MEDTR
228
0
24757
TrEMBL
other Location (Reliability: 2 )
A0A2P6QBQ6_ROSCH
301
0
33116
TrEMBL
Chloroplast (Reliability: 3 )
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13800
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x * 13800 + x * 15200 + x * 32500, SDS-PAGE
15200
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x * 13800 + x * 15200 + x * 32500, SDS-PAGE
32500
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x * 13800 + x * 15200 + x * 32500, SDS-PAGE
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?
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x * 13800 + x * 15200 + x * 32500, SDS-PAGE
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x * 13800 + x * 15200 + x * 32500, SDS-PAGE
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monomer
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1 * 33500, SDS-PAGE
monomer
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1 * 33800, SDS-PAGE
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glycoprotein
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two N-linked oligosaccharide chains, 8% by weight, at Asn99 and Asn156
glycoprotein
Asn99 and Asn156 are occupied by the glycans (Man)3(xyl)1(Fuc)1(GlcNAc)2 and (Man)3(Xyl)1(Fuc)1(GlcNAc)3 in a ratio of 7:1. Both glycan s are xylose containing biantennary complex types that share the common core structural unit, Man1-6(Man1-3)(Xyl1-2)Man1-4GlcNAc1-4(Fuc1-3)GlcNAc
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vapor difusion method with hanging-drop geometry
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2 - 12
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purified native enzyme, at least 120 min, stable
731160
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-20 - 60
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purified native enzyme, at least 120 min, stable
40 - 65
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purified native enzyme, pH 7.0, 2 h, stable
5
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half-life of 2.1 d decreasing to 20 min at 30°C, addition of ascorbate increases the half-time to 20 d, acetone powder preperations from ginger yielded a half-time of 18 months
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ascorbic acid, EDTA, and cysteine stabilize the purified enzyme
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pH 7.0, potassium phosphate buffer and 10 mM cysteine in combination with 5 mM EDTA as stabilizer are most effective conditions during enzyme extraction
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-20-60, purified native enzyme, at least 120 min, stable
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4°C, more than half of the initial activity is lost after 1 day of storage and after 4 days of storage, only 10.4% of the initial activity remain
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?20°C, purified lyophilized enzyme, retains activity for 22 months
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native enzyme 14.91fold from rhizomes by ammonium sulfate fractionation, tert-butanol precipitation at 25°C and pH 7.0 using the interfacial precipitateand the aqueous phase, and ultrafiltration, method optimization
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native enzyme from rhizomes by ammonium sulfate fractionation and dialysis
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native enzyme from rhizomes by ammonium sulfate fractionation, anion exchange chromatography, SDS-PAGE, and gel filtration
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native enzyme from rhizomes by saturation ammonium sulfate fractionation and anion exchange chromatography to homogeneity
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partially purified 252fold with a recovery of 61%, ion exchange chromatography
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purification via a three-phase partitioning system
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ultrasonic-assisted liquid-liquid microextraction of the proteases from ginger and sodom apple using natural deep eutectic solvents, NADES. Selective partitioning of NADES-assisted microextraction yields more protease in NADES-enriched top phase. Maximum yield is achieved with 25% (v/v) of NADES, 15% (w/v) of source concentration and ultrasound temperature and time as 35°C and 10 min, respectively
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nutrition
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meat tenderizing agent, stability of the enzyme can be greatly improved, increasing its attractiveness as a commercial product
food industry
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application of enzyme in food industry for cheese-making or meat tenderization. Optimization of purification protocol via three-phase partitioning system
food industry
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zingipain can hydrolyze the gelatin from fish skin to peptides with low average molecular weights (below 690 Da) more efficiently than that from pig skin, pig bone and bovine skin. All gelatin hydrolysates show higher antioxidative activities than non-hydrolysed gelatins. Fish skin gelatin hydrolysate obtained using ginger protease exhibits the highest degree of hydrolysis (13.08%) and antioxidant activity towards 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical (97.21%) and lipid peroxidation (48.46%)
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Choi K.H.; Laursen R.A.
Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale
Eur. J. Biochem.
267
1516-1526
2000
Zingiber officinale (P82474), Zingiber officinale
brenda
Choi, K.H.; Laursen, R.A.; Allen, K.N.
The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale
Biochemistry
38
11624-11633
1999
Zingiber officinale
brenda
Dai, Jingquan; Huang, Xuesong
Purification of ginger protease
Food College, Shandong Agricultural University, Tai'an, Peop. Rep. China. Shipin Kexue (Beijing, China)
24
73-79
2003
Zingiber officinale
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brenda
Laursen, R.A.
Zingiber cysteine proteinases
Handbook of Proteolytic Enzymes (Barrett, A.J., Rawlings, N.D., Woessner, J.F., eds)
2
1151-1152
2004
Zingiber officinale
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brenda
Adulyatham, P.; Owusu-Apenten, R.
Stabilization and partial purification of a protease from ginger rhizome (Zingiber offinale Roscoe)
J. Food Sci.
70
C231-C234
2005
Zingiber officinale
brenda
Karnchanatat, A.; Tiengburanatam, N.; Boonmee, A.; Puthong, S.; Sangvanich, P.
Zingipain, A cysteine protease from Zingiber ottensii Valeton rhizomes with antiproliferative activities against fungi and human malignant cell lines
Prep. Biochem. Biotechnol.
41
138-153
2011
Zingiber ottensii, Zingiber ottensii Valeton
brenda
Rungsaeng, P.; Sangvanich, P.; Karnchanatat, A.
Zingipain, a ginger protease with acetylcholinesterase inhibitory activity
Appl. Biochem. Biotechnol.
170
934-950
2013
Zingiber officinale
brenda
Nafi, A., Foo, H. L., Jamilah, B., Ghazali. H. M.
Properties of proteolytic enzyme from ginger (Zingiber officinale Roscoe)
Int. Food Res. J.
20
363-368
2013
Zingiber officinale
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brenda
Gagaoua, M.; Hoggas,N.; Hafid, K.
Three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes
Int. J. Biol. Macromol.
73
245-252
2015
Zingiber officinale
brenda
Nafi, A.; Hooi Ling, F.; Bakar, J.; Ghazali, H.M.
Partial characterization of an enzymatic Extract from Bentong Ginger (Zingiber officinale var. Bentong)
Molecules
19
12336-12348
2014
Zingiber officinale
brenda
Gagaoua, M.; Hafid, K.; Hoggas, N.
Data in support of three phase partitioning of zingibain, a milk-clotting enzyme from Zingiber officinale Roscoe rhizomes
Data Brief
6
634-639
2016
Zingiber officinale
brenda
Zheng, L.; Yu, H.; Wei, H.; Xing, Q.; Zou, Y.; Zhou, Y.; Peng, J.
Antioxidative peptides of hydrolysate prepared from fish skin gelatin using ginger protease activate antioxidant response element-mediated gene transcription in IPEC-J2 cells
J. Funct. Foods
51
104-112
2018
Zingiber officinale
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brenda
Balaraman, H.; Rathnasamy, S.
Selective purification of protease from ginger and sodom apple by ultrasound assisted liquid-liquid microextraction using natural deep eutectic solvent
Microchem. J.
150
104132
2019
Zingiber officinale
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brenda
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