Information on EC 3.4.22.67 - zingipain

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The expected taxonomic range for this enzyme is: Zingiber

EC NUMBER
COMMENTARY
3.4.22.67
-
RECOMMENDED NAME
GeneOntology No.
zingipain
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
preferential cleavage of peptides with a proline residue at the P2 position
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C01.017
-
-
-
-
cysteine proteinase GP-II
-
-
-
-
F50
Zingiber ottensii Valeton
-
-
-
ginger protease
-
-
ginger protease II
-
-
GP-II
-
-
-
-
zingibain
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-
CAS REGISTRY NUMBER
COMMENTARY
246044-91-7
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Zingiber ottensii Valeton
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
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
Zingiber ottensii Valeton
-
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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SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetoacetate decarboxylase + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
?
show the reaction diagram
-
-
-
-
?
azocasein + H2O
?
show the reaction diagram
Zingiber ottensii, Zingiber ottensii Valeton
-
-
-
-
?
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
-
-
-
-
?
Myoglobin + H2O
?
show the reaction diagram
-
-
-
-
?
Lysozyme + H2O
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme prefers to cleave peptide bonds at which Pro is in the P2 position
-
-
-
additional information
?
-
P82474, -
enzyme prefers to cleave peptide bonds at which Pro is in the P2 position
-
-
-
additional information
?
-
-
initial cleavage is at peptide bonds with P2 Pro
-
-
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INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
iodoacetic acid
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Zingiber ottensii Valeton
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
34800
-
-
SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 13800 + x * 15200 + x * 32500, SDS-PAGE
?
Zingiber ottensii Valeton
-
x * 13800 + x * 15200 + x * 32500, SDS-PAGE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
P82474
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 ACCESSION NO.
LITERATURE
at 2.1 A resolution
-
vapor difusion method with hanging-drop geometry
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TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partially purified 252fold with a recovery of 61%, ion exchange chromatography
-
native enzyme from rhizomes by ammonium sulfate fractionation, anion exchange chromatography, SDS-PAGE, and gel filtration
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APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
meat tenderizing agent, stability of the enzyme can be greatly improved, increasing its attractiveness as a commercial product