Information on EC 3.4.22.67 - zingipain

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The expected taxonomic range for this enzyme is: Zingiber

EC NUMBER
COMMENTARY hide
3.4.22.67
-
RECOMMENDED NAME
GeneOntology No.
zingipain
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential cleavage of peptides with a proline residue at the P2 position
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
246044-91-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme has sequence similarity with zingipain-1 from Zingiber officinalis
physiological function
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
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
INHIBITORS
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
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no activating or inhibitory, but a stabilizing effect by EDTA, no inhibition by K+ and Na+
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
-
-
additional information
-
no activating or inhibitory, but a stabilizing effect by EDTA
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Km and Vmax values are 0.21 mg/ml and 34.48 mg/m/min, respectively, with substrate azocasein
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.005
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purified native enzyme, substrate bovine casein, pH 7.0, 40C
27.6
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purified native enzyme, substrate azocasein, pH 7.0, 60C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
-
assay at
7
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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
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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
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activity range, profile overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.38
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isoelectric focussing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33500
-
native PAGE
33800
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native PAGE
34800
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
at 2.1 A resolution
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vapor difusion method with hanging-drop geometry
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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
5
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half-life of 2.1 d decreasing to 20 min at 30C, addition of ascorbate increases the half-time to 20 d, acetone powder preperations from ginger yielded a half-time of 18 months
40 - 65
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purified native enzyme, pH 7.0, 2 h, stable
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20-60, purified native enzyme, at least 120 min, stable
-
4C, 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
-
?20C, purified lyophilized enzyme, retains activity for 22 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 14.91fold from rhizomes by ammonium sulfate fractionation, tert-butanol precipitation at 25C 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 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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
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meat tenderizing agent, stability of the enzyme can be greatly improved, increasing its attractiveness as a commercial product