3.4.22.65: peptidase 1 (mite)
This is an abbreviated version!
For detailed information about peptidase 1 (mite), go to the full flat file.
Word Map on EC 3.4.22.65
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3.4.22.65
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allergic
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asthma
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ige
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dermatophagoides
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pteronyssinus
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children
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home
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asthmatic
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atopic
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farinae
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airway
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indoor
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immunotherapy
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mattress
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bronchial
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rhinitis
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inhale
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prick
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allergen-specific
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floor
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carpet
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bedroom
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dermatitis
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humid
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hyperresponsiveness
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airborne
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household
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houses
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cockroach
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aeroallergens
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vacuum
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wheeze
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house-dust
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ige-binding
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cleaner
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ras
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blomia
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anti-der
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allergen-induced
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rhinoconjunctivitis
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component-resolved
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mite-induced
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radioallergosorbent
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diagnostics
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hdm-induced
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hypoallergenic
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pharmacology
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nonatopic
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medicine
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wheal
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immunocap
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dander
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skin-prick
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drug development
- 3.4.22.65
-
allergic
- asthma
- ige
- dermatophagoides
- pteronyssinus
- children
-
home
-
asthmatic
-
atopic
- farinae
- airway
-
indoor
-
immunotherapy
-
mattress
- bronchial
- rhinitis
-
inhale
-
prick
-
allergen-specific
-
floor
-
carpet
-
bedroom
- dermatitis
-
humid
-
hyperresponsiveness
-
airborne
-
household
-
houses
- cockroach
-
aeroallergens
-
vacuum
-
wheeze
-
house-dust
-
ige-binding
-
cleaner
- ras
- blomia
-
anti-der
-
allergen-induced
-
rhinoconjunctivitis
-
component-resolved
-
mite-induced
-
radioallergosorbent
- diagnostics
-
hdm-induced
-
hypoallergenic
- pharmacology
-
nonatopic
- medicine
-
wheal
-
immunocap
-
dander
-
skin-prick
- drug development
Reaction
broad endopeptidase specificity =
Synonyms
allergen Der f 1, allergen Der f1, allergen Der p, allergen Der p 1, allergen Der p1, CO1.073, Der f 1, Der f1, Der p 1, Der p 7, Der p1, dust mite allergen Der p 7, dust mite peptidase allergen Der p 1, house dust mite allergen, house dust mite allergens, major house dust mite allergen, mite allergen, mite major group 1 allergens, pro-Der f1, ProDer f 1, ProDer p 1
ECTree
3.4.22.65 peptidase 1 (mite)Advanced search results
results (
results (Engineering
Engineering on EC 3.4.22.65 - peptidase 1 (mite)
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C104S/N53Q
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proform of mutant enzyme is not efficiently secreted into culture medium
C118S/N53Q
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proform of mutant enzyme is not efficiently secreted into culture medium
C32S/C72S/N63Q
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proform of mutant enzyme is not efficiently secreted into culture medium
C32S/N53Q
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proform of mutant enzyme is not efficiently secreted into culture medium
C35S/N53Q
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proform of mutant enzyme is efficiently secreted into culture medium. The secreted pro-C35S/N53Q is converted to the mature form by treatment in acidic conditions. Cysteine protease activity of the processed C35S/N53Q is lower than that of native Der f1 but significantly higher than that of the proenzyme
C4S/N53Q
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proform of mutant enzyme is not efficiently secreted into culture medium
C66S/C104S/N53Q
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proform of mutant enzyme is not efficiently secreted into culture medium
C66S/N53Q
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proform of mutant enzyme is not efficiently secreted into culture medium
C72S/N53Q
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proform of mutant enzyme is not efficiently secreted into culture medium
N53Q
C132V
site-directed mutagenesis, Der p 1 catalytic site mutant
N52Q
additional information
N53Q
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the proform of N53Q is efficiently secreted into culture supernatant and processed to be of almost the same molecular weight as native enzyme by treatment in acidic conditions
N52Q
mutant with disrupted N-glycosylation motif in the prodomain
N52Q
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mutant with disrupted N-glycosylation motif in the prodomain, decreases the productivity and accelerates the maturation
N52Q
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mutant with disrupted N-glycosylation motif in the prodomain, lower productivity
N52Q
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molecular weight identical with that of natural allergen
additional information
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lysylendopeptidase-treated reDER f1 E(-1)K shows some differences in protease activity and reactivity with lectins: GlcNAc is contained at the non-reducing terminus of the sugar chains of native Der f1 but not of lysylendopeptidase-treated reDEr f1 E(-1)K. Lysylendopeptidase-treated reDEr f1 E(-1)K reacts with Lens culinaris agglutinin but native Der f1 does not, suggesting that fucose is connected with GlcNAc, bound to an asparagine residue, but not of native Der f1. Their N-terminal amino acid and the IgE-binding activity are the same as those of the native one
additional information
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mutant Der f 1-N53Q, in which the N-glycosylation motif within the mature sequence is disrupted
additional information
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mutant Der f 1-N53Q, in which the N-glycosylation motif within the mature sequence is disrupted
additional information
construction of a chimeric allergen R8, derived from the major allergen group 1 of house dust mites species, Dermatophagoides farinae and Dermatophagoides pteronyssinus
additional information
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hybrid molecules from parts of Der p 1 and Der p2 are constructed
additional information
development of chimeras assembling Der p 1 and Der p 2 allergens. Mutations in the Der p 1 catalytic site are also engineered
additional information
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development of chimeras assembling Der p 1 and Der p 2 allergens. Mutations in the Der p 1 catalytic site are also engineered
additional information
construction of a chimeric allergen R8, derived from the major allergen group 1 of house dust mites species, Dermatophagoides farinae and Dermatophagoides pteronyssinus
