Information on EC 3.4.21.49 - hypodermin C

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The expected taxonomic range for this enzyme is: Hypoderma

EC NUMBER
COMMENTARY hide
3.4.21.49
-
RECOMMENDED NAME
GeneOntology No.
hypodermin C
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of proteins including native collagen at -/-Ala bond leaving an N-terminal (75%) and a C-terminal (25%) fragment
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY hide
122191-36-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
additional information
-
identification of the DNA binding sites of the enzyme using an electrophoretic mobility shift asay
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Azocoll + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
Collagen + H2O
?
show the reaction diagram
guinea pig complement C3 + H2O
?
show the reaction diagram
-
recombinant enzyme, degradation
-
-
?
oxidized insulin B chain + H2O
?
show the reaction diagram
-
major cleavage at Arg22-Gly23 and Lys29-Ala30 bonds
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
Collagen + H2O
?
show the reaction diagram
-
enzyme functions in degradation of collagen in the connective tissue of the host, so that the larvae of Hypoderma lineatum can feed on the degradation products and migrate
-
-
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diisopropylfluorophosphate
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
8 - 8.5
-
hydrolysis of collagen
8
-
hydrolysis of azocoll
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 11
-
pH 5.0: abouut 30% of maximal activity, pH 11.0: about 80% of maximal activity
6 - 10
-
pH 6.0: about 30% of maximal activity, pH 10.0: about 80% of maximal activity, hydrolysis of collagen
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is secreted by the first-instar larvae
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17800
-
gel filtration
22000
-
low-speed equilibrium sedimentation
24000
-
1 * 24000, SDS-PAGE
25223
-
x * 25223, calculation from amino acid sequence
28561
-
x * 28561, calculation from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 24000, SDS-PAGE
additional information
-
structural study of the active site
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
-
the enzyme appears to be faintly glycosylated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
2 h, stable below
70
-
2 h, no loss of activity at or below
75
-
20 min, 55% loss of activity. 2 h, complete inactivation
90
-
2 h, about 50% loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, recombinant expression in COS7 cells using the pEF1a-IRES-AcGFP expression vector. COS7 cells stably expressing the enzyme are more resistant to lysis by guinea pig complement C3 than the control cells
-
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
medicine
-
dynamics of circulating hypodermin C in previously infested cattle resemble those in previously uninfested cattle. Development of a significant immune response during the primary infestation that is reflected in the rapid and substantial production of antibodies upon re-infestation, thus migrating first instars may induce significant reduction in host immune response