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Information on EC 3.4.22.67 - zingipain and Organism(s) Zingiber officinale and UniProt Accession P82474

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.67 zingipain
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Zingiber officinale
UNIPROT: P82474 not found.
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The taxonomic range for the selected organisms is: Zingiber officinale
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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preferential cleavage of peptides with a proline residue at the P2 position
Synonyms
gp-ii, zingibain, ginger protease, zingipain, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C01.017
-
-
-
-
cysteine proteinase GP-II
-
-
-
-
ginger protease
-
-
ginger protease II
-
-
GP-II
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
246044-91-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetoacetate decarboxylase + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
bovine casein + H2O
?
show the reaction diagram
-
-
-
-
?
Bovine serum albumin + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
-
-
-
-
?
Gelatin + H2O
?
show the reaction diagram
-
-
-
-
?
Lysozyme + H2O
?
show the reaction diagram
-
-
-
-
?
Myoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates
Cu2+
-
activates at 1-10 mM
Fe2+
-
activates at 1 mM, inhibits at 10 mM
Hg2+
-
activates at 1 mM, complete inhibition at 5-10 mM
K+
-
activates
Mg2+
-
activates at 1 mM, inhibits at 10 mM
Mn2+
-
activates at 1-10 mM
Na+
-
activates
Zn2+
-
activates at 1 mM, inhibits at 10 mM
additional information
-
the purified enzyme is highly stable against numerous metal ions
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
-
Al3+
-
slight inhibition
Ba2+
-
slight inhibition
Ca2+
-
slight inhibition
Cd2+
-
strong inhibition
EDTA
-
about 60% inhibition at 1-10 mM
Fe2+
-
activates at 1 mM, inhibits at 10 mM
iodoacetamide
-
-
iodoacetic acid
-
-
mercurial
-
-
Mn2+
-
slight inhibition
NEM
-
strong inhibition
o-phenanthroline
-
-
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane
-
-
additional information
-
no activating or inhibitory, but a stabilizing effect by EDTA, no inhibition by K+ and Na+
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
-
-
additional information
-
no activating or inhibitory, but a stabilizing effect by EDTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
casein
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.005
-
purified native enzyme, substrate bovine casein, pH 7.0, 40°C
27.6
-
purified native enzyme, substrate azocasein, pH 7.0, 60°C
3573
-
pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
assay at
7
-
broad optimum at pH 6.0-7.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8.5
-
activity range, profile overview
4.5 - 9.5
-
activity range, profile overview
5 - 9.5
-
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 80
-
activity range, profile overview
25 - 80
-
activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.38
-
isoelectric focussing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme has sequence similarity with zingipain-1 from Zingiber officinalis
additional information
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CPGP2_ZINOF
221
0
23922
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33500
-
native PAGE
33800
-
native PAGE
34800
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
glycoprotein
-
two N-linked oligosaccharide chains, 8% by weight, at Asn99 and Asn156
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2.1 A resolution
-
vapor difusion method with hanging-drop geometry
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 12
-
purified native enzyme, at least 120 min, stable
731160
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20 - 60
-
purified native enzyme, at least 120 min, stable
40 - 65
-
purified native enzyme, pH 7.0, 2 h, stable
5
-
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ascorbic acid, EDTA, and cysteine stabilize the purified enzyme
-
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
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20-60, purified native enzyme, at least 120 min, stable
-
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
-
?20°C, purified lyophilized enzyme, retains activity for 22 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
native enzyme from rhizomes by ammonium sulfate fractionation and dialysis
-
native enzyme from rhizomes by saturation ammonium sulfate fractionation and anion exchange chromatography to homogeneity
-
partially purified 252fold with a recovery of 61%, ion exchange chromatography
-
purification via a three-phase partitioning system
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
nutrition
-
meat tenderizing agent, stability of the enzyme can be greatly improved, increasing its attractiveness as a commercial product
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Rungsaeng, P.; Sangvanich, P.; Karnchanatat, A.
Zingipain, a ginger protease with acetylcholinesterase inhibitory activity
Appl. Biochem. Biotechnol.
170
934-950
2013
Zingiber officinale
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team