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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Substrates Products
Substrates Products on EC 3.4.22.65 - peptidase 1 (mite)
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REACTION DIAGRAM
(2-aminobenzoyl)-Val-Ala-norLeu-Ser-Tyr(3-NO2)-Asp + H2O
?
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ADZ 50,059
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-
?
2-aminobenzoic acid-Val-Ala-Nle-Ser-(3-nitro)-tyrosinyl-aspartamide + H2O
?
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-
-
-
?
alpha1-antitrypsin + H2O
?
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recombinant Der p 1 previously activated with L-cysteine or DTT
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-
?
butyloxycarbonyl-Gln-Ala-Arg-4-methylcoumaryl-7-amide + H2O
butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
?
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-
-
-
?
butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
butyloxycarbonyl-Gln-Ala-Arg-MCA + H2O
butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
butyloxycarbonyl-Gln-Gly-Arg-MCA + H2O
butyloxycarbonyl-Gln-Gly-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
butyloxycarbonyl-Phe-Ser-Arg-MCA + H2O
butyloxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
butyloxycarbonyl-Val-Leu-Lys-MCA + H2O
butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
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-
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?
chestnut cystatin + H2O
?
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specific proteolytic cleavage between Gly6 and Val7, giving rise to a noninhibitory processed protein. Not cleaved by Der f 1 from Dermatophygoides farinae
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-
?
Der p 1 propiece + H2O
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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
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-
?
human alpha1-antitrypsin + H2O
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cleaved by Der f 1-N53Q but not without its activation
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-
?
mas-related G-protein-coupled receptor X1 + H2O
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human protein
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-
?
N-succinyl-Ala-Pro-Ala-7-amido-4-methylcoumarin
N-succinyl-Ala-Pro-Ala + 7-amino-4-methylcoumarin
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-
-
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?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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more efficiently hydrolyzed than N-succinyl-Ala-Pro-Ala-7-amido-4-methylcoumarin
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-
?
N-succinyl-Leu-Leu-Val-Tyr-7-amido-4-methylcoumarin + H2O
N-succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
succinyl-Leu-Leu-Val-Tyr-MCA + H2O
succinyl-Leu-Leu-Val-Tyr + 7-amino-4-methylcoumarin
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-
-
-
?
Z-Phe-Arg-4-methylcoumarin 7-amide + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
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-
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?
Azocoll + H2O
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collagen substrate, Der f 1-N53Q proteolytically active
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-
?
butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
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-
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?
butyloxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
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short synthetic substrate
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-
?
butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
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-
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?
butyloxycarbonyl-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
butyloxycarbonyl-Val-Leu-Lys + 7-amino-4-methylcoumarin
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more efficiently hydrolyzed than N-succinyl-Ala-Pro-Ala-7-amido-4-methylcoumarin
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-
?
CD23 + H2O
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CD23 is a calcium-dependent type II integral membrane protein. CD23 from the surface of cultured human B cells is cleaved at two sites: Ser155-Ser156 and Glu298-Ser299 to produce a 17000 Da fragment containing the lectin domain and only part of the C-terminal tail. No such effect is demonstrable with mouse CD23
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?
CD23 + H2O
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cleaves CD23 from the surface of cultured human B cells. The cleavage of the receptor from the B cell sulface is associated with a parallel increase in soluble CD23
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?
CD23 + H2O
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Der p 1 in addition to being highly immunogenic may up-regulate IgE synthesis by virtue of its ability to cleave CD23
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?
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cleaved by Der f 1-N53Q and natural Der f 1 on the cell surface in a time- and dose dependent manner
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?
human CD25 + H2O
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cleaved by Der f 1-N53Q and natural Der f 1 on the cell surface in a time- and dose dependent manner
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-
?
lung surfactant protein A + H2O
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degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen
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-
?
lung surfactant protein D + H2O
?
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degradation of lung surfactant protein A and lung surfactant protein D is associated with diminished binding to carbohydrates and to Dermatophagoides pteronyssinus allergen 1 itself and diminishes capacity to agglutinate bacteria. The degradation and consequent inactivation of lung surfactant protein A and lung surfactant protein D may be a novel mechanism to account for the potent allergenicity of the dust mite allergen
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-
?
?
human protein
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-
?
mas-related G-protein-coupled receptor C11 + H2O
?
mouse protein
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-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
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-
-
?
N-tert-butoxycarbonyl-Gln-Ala-Arg-7-amido-4-methylcoumarin + H2O
N-tert-butoxycarbonyl-Gln-Ala-Arg + 7-amino-4-methylcoumarin
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-
-
-
?
Der p 3 + Der p 3 propeptide
activation
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-
?
pro-Der p 3 + H2O
Der p 3 + Der p 3 propeptide
activation, the enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen
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-
?
Der p 6 + Der p 6 propeptide
activation
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-
?
pro-Der p 6 + H2O
Der p 6 + Der p 6 propeptide
pro-Der p 6 zymogen is recombinantly produced in Pichia pastoris, activation mechanism analysis by mite protease Der p 1, overview. The enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen. The N-terminal sequence of rDer p 6 is V35IGGDQ. The propeptide of proDer p 6 inhibits the proteolytic activity of protease Der p 6, but once cleaved, it is degraded by the protease
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-
?
Der p 9 + Der p 9 propeptide
activation
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-
?
pro-Der p 9 + H2O
Der p 9 + Der p 9 propeptide
activation, the enzyme Der p 1 cleaves the substrate between the P1 and P'1 positions of the activation site of the zymogen
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?
?
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mature recombinant enzyme shows the same IgE binding activity as the native enzyme
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additional information
?
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allergen from Dermatophagoides farinae
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-
?
additional information
?
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recombinant Der f 1 activated with L-cysteine reduces the barrier function of the skin in dose- and time-dependent manners. The reduction is dependent on its proteolytic activity
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?
additional information
?
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development of a highly sensitive and specific fiber-optic chemifluorescent immunoassay (ELISA) for the detection of airborne enzyme allergen Der f1. The Der f1 concentration is measured on the basis of the intensity of fluorescence amplified by an enzymatic reaction between the labeled enzyme by a detection antibody and a fluorescent substrate 2,2'-azinobis [3-ethylbenzothiazoline-6-sulfonic acid]-diammonium salt of horse radish peroxidase, overview
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?
additional information
?
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development of a highly sensitive and specific fiber-optic chemifluorescent immunoassay (ELISA) for the detection of airborne enzyme allergen Der f1. The Der f1 concentration is measured on the basis of the intensity of fluorescence amplified by an enzymatic reaction between the labeled enzyme by a detection antibody and a fluorescent substrate 2,2'-azinobis [3-ethylbenzothiazoline-6-sulfonic acid]-diammonium salt of horse radish peroxidase, overview
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?
additional information
?
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Der p 1 is the most immunodominant allergen involved in the expression of dust mite-specific immunoglobulin (Ig)E-mediated hypersensitivity. The proteolytic activity of Der p 1 is a major contributor to its allergenicity. Cysteine protease activity of Der p 1 enhances total IgE production
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?
additional information
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cysteine protease activity of Der p 1 enhances total IgE production, apart from increasing Der p 1-specific IgE. This allergen may play a central role in destabilizing the micro-environment within target tissues to one that is pro-allergic, and thus aid in the initiation and propagation of the allergic cascade
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?
additional information
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the efficient in vivo responses, including production of IgE and IgG against the highly purified rDer p 1, are dependent on the cysteine protease activity in mice. The three types of rDer p 1 differing in function or structure elicit distinctly different immune responses
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?
additional information
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the house dust mite allergen Der p 1 stimulates the expression of interleukin-8 in human airway epithelial cells via a proteinase-activated receptor-2-independent mechanism
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additional information
?
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house dust mite major allergens Der p 1 and Der p 5 activate human airway-derived epithelial cells by protease-dependent and protease-independent mechanisms
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additional information
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Der p 7 binds a bacterially-derived lipid product, a common feature of some allergens, ligand binding analysis by NMR analysis
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?