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
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Posttranslational Modification
Posttranslational Modification on EC 3.4.22.65 - peptidase 1 (mite)
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glycoprotein
proteolytic modification
glycoprotein
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the wild-type recombinant enzyme is more highly glycosylated than the native enzyme
glycoprotein
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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
glycoprotein
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N-glycosylation is essential for secretion in insect Sf9 cells but not in Pichia pastoris
glycoprotein
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N-glycosylation of the prosequences decelerated the maturation. Systems using Pro-Der p 1 without the prodomain glycosylation are useful for the efficient preparation of a recombinant mature allergen
glycoprotein
different levels of glycosylation or isozymes
glycoprotein
analysis of the glycosylation pattern and comparison to other allergens, mannosylation appears to be a dominant feature among allergens, overview. The main dominant sugars on these allergens are 1-2, 1-3 and 1-6 mannose, the sugar part of the enzyme is recognized by lectins from Datura stramonium lectin, Arachis hypogaea, and Sambucus nigra. Sodium periodate deglycosylation of natural and recombinant enzyme Der p 1 resulting in a significant decrease in the uptake of both Der p 1 preparations into dendritic cells. The recombinant enzyme shows a higher degree of mannans compared to the native enzyme
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the presence of the pro-sequence is inhibitory to the IgE-binding activity of Der f1
proteolytic modification
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the removal of the pro-sequence is necessary for the cysteine protease activity. Acid treatment of the renatured pro Der f1 results in the autocatalytic removal of the pro-sequence. The obtained mature form of Der f1 binds IgE in patient sera and induces the release of histamine from peripheral blood leukocytes equally to native Der f1
proteolytic modification
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the N-terminal sequences of the secreted proteins are determined to start from -59 or -78, downstream from the putative signal-cleavage site in the prosequence of Der f 1. Those of processed proteins are determined to start from -2 or 1, two residues upstream from or at the N-terminus of native Der f 1. The prosequence is removed autocatalytically by dialysis against acidic buffer
proteolytic modification
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the processed reDer f1 E(-1)K can be obtained after lysylendopeptidase and endoglycosidase Hf treatment
proteolytic modification
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the proforms of Der p 1 and Der f1 differ in the N-terminal sequences
proteolytic modification
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contribution of the N-terminal region of the Der p 1 prosequence including the N-glycosylation site, Asn(-65), on effective inhibition of proteolytic activity in pro-Der p 1
proteolytic modification
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the Der p 1 propiece is a potent competitive inhibitor of Der p 1. The Der p 1 propiece behaves as a substrate and is fully degraded during this interaction. The rapid inactivation of Der p 1 prodomain is a mechanism that may contribute to the potency of this allergen
proteolytic modification
the Der p 1 enzyme propeptide of 80 amino acids plays an essential role in zymogen folding as an intramolecular chaperone and in the inhibition of its own enzymatic activity