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Information on EC 3.4.22.65 - peptidase 1 (mite)

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.65 peptidase 1 (mite)
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This record set is specific for:
UNIPROT: Q58A71 not found.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
broad endopeptidase specificity
the proteolytic activity of Der f 1 is a major contributor to its allergenicity. Cysteine protease activity of Der p 1 enhances total IgE production
Synonyms
der p 1, mite allergen, der f 1, house dust mite allergen, der p1, house dust mite allergens, der f1, der p 7, allergen der p 1, allergen der p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
allergen Der f1
-
-
-
-
CO1.073
-
-
-
-
Der f 1
-
-
-
-
Der p 1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme is a group 1 mite allergen
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q58A71_DERFA
321
0
36391
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
x * 34000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type enzyme and chimeric allergen R8 from Nicotiana benthamiana leaves by affinity chromatography to homogeneity under denaturing conditions
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of C-terminally His6-tagged wild-type enzyme and chimeric allergen R8, derived from the major allergen group 1 of house dust mites species, Dermatophagoides farinae and Dermatophagoides pteronyssinus, in leaves of Nicotiana benthamiana via transfection with Agrobacterium tumefaciens strain GV3101
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type enzyme and chimeric allergen R8 from Nicotiana benthamiana leaves after purification by affinity chromatography under denaturing conditions, refolding by dialysis against decreasing concentrations of urea
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cui, Y.; Zhou, P.; Peng, J.; Peng, M.; Zhou, Y.; Lin, Y.; Liu, L.
Cloning, sequence analysis, and expression of cDNA coding for the major house dust mite allergen, Der f 1, in Escherichia coli
Braz. J. Med. Biol. Res.
41
380-388
2008
Dermatophagoides farinae (Q58A71), Dermatophagoides farinae
Manually annotated by BRENDA team
Li, C.; Jiang, Y.; Guo, W.; Liu, Z.
Production of a chimeric allergen derived from the major allergen group 1 of house dust mite species in Nicotiana benthamiana
Hum. Immunol.
74
531-537
2013
Dermatophagoides pteronyssinus (P08176), Dermatophagoides farinae (Q58A71)
Manually annotated by BRENDA team