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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

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 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.65 peptidase 1 (mite)

Cloned

Cloned on EC 3.4.22.65 - peptidase 1 (mite)

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of an isopropyl-beta-D-thiogalactopyranoside-inducible expression plasmid to produce the pro-form of Der f1 in Escherichia coli
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Der p 1.0124 (according to the IUIS-WHO Allergen Nomenclature Subcommittee)
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DNA and amino acid sequence determination and analysis of the cDNA sequence encoding proenzyme pro-Der f1, recombinant expression od Strep-tagged proenzyme in Escherichia coli in inclusion bodies from vector pET-44a
DNA fragment encoding precursor-type recombinant Der f1 E(-1)K, which has the C-terminal amino acid of the pro-sequence, Glu, changed to Lys, expression in Aspergillus oryzae
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expressed in Pichia pastoris
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expressed in Saccharomyces cerevisiae
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expression and maturation of prepro-Der p 1 and its mutants in Pichia pastoris. Maturation systems using Pro-Der p 1 without the prodomain glycosylation are useful for the efficient preparation of a recombinant mature allergen
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expression in Escherichia coli
expression in Pichia pastoris
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expression in Pichia pastoris X-33
expression of Der p 7-MBP fusion protein and His6-tagged Der p 7 in Escherichia coli Rosetta2(DE3) pLacI cells
expression of His-tagged fusion proteins encompassing Der p 2 with either mature or proDer p 1 in Escherichia coli strain BL21 (DE3) and Origami2 (DE3), or in Pichia pastoris strain GS115 or X33. Four fusion proteins are expressed in Escherichia coli as inclusion bodies, whereas only chimeras comprising proDer p 1 are obtained in yeast
I-Der p 1 gene, cDNA isolation, DNA and amino acid sequence determination and analysis, detection of 11 polymorphisms to the sequence of peptidase 1, DERP1, UniProt ID P08176, sequence comparison, PVX-mediated expression of immunologically active mature form I-rDer p 1 in Nicotiana benthamiana plants using a Agrobacterium tumefaciens strain GV3101-mediated transfection strategy, the recombinant enzyme comprises the N-terminal 222 amino acids which corresponds to the mature form of I-Der p 1 after proteolytic cleavage, the C-terminus is expressed as FLAG-tagged protein
preparation described elsewhere, proform secreted in Pichia pastoris culture supernatant and converted into their prosequence-removed mature form, recombinant protein exhibits cysteine protease activity but no serine protease activity
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production of recombinant enzyme in insect cells using a baculovirus expression system
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recombinant Der f1 that is produced using a baculovirus expression sytem contains pro-sequences of different length. Most of theses can be removed by acid treatment. The N-terminal amino acids of the acid-treated recombinant enzyme are uniform. A method for processing of the pro-sequence has been developed by producing reDer f1 E(-1)K with baculovirus expression system in which the carboxy terminal amino acid of the pro-sequence (glutamate) is replaced by lysine. Addition of lysylendopeptidase into the culture medium leads to processing of the pro-sequence of reDer f1 E(-1)K
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recombinant expression in Pichia pastoris
recombinant expression of C-terminally His6-tagged 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
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
recombinant ProDer p 1 from CHO cells
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recombinant proforms secreted into culture supernatant of Pichia pastoris cells and converted into prosequence-removed mature form Der p 1-WT
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recombinant proforms were secreted into the culture of Pichia pastoris transfectant cells and converted into the prosequence-removed mature forms by means of dialysis against an acidic buffer
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the preproforms of Der f 1 and a mutant N53Q, whose consensus motif for N-glycosylation is disrupted, are expressed in Pichia pastoris
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the propiece of Der p 1 is PCR cloned and expressed in Escherichia coli
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wild-type and mutant enzyme N52Q, expression in Pichia pastoris
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wild-type pro-Der f1 is secreted to culture medium of baculovirus-transfeceted SF9 cells, pro-N53Q is not secreted in insect Sf9 cells although secreted in Pichia pastoris
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