Peptidase 1 (mite)

Peptidase 1 (mite)
Crystal structure of Der p 1 allergen[1] from pdb entry 3F5V
Identifiers
EC no.3.4.22.65
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
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MetaCycmetabolic pathway
PRIAMprofile
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Peptidase 1 (mite) (EC 3.4.22.65), also known as endopeptidase 1 (mite), is an enzyme found in various species of mites.[2][3] This enzyme exhibits cysteine protease activity with broad endopeptidase specificity.[4]

The various forms of peptidase 1 pertaining to individual mite species comprise the group 1 mite allergens.[5] Following the naming conventions of allergens, these peptidase 1 variants include Der p 1 of the European house dust mite Dermatophagoides pteronyssinus;[6] Der f 1 of the American house dust mite Dermatophagoides farinae;[1] Eur m 1 of the Mayne's house dust mite Euroglyphus maynei;[7] and Pso o 1 of the sheep scab mite Psoroptes ovis.[8] The group 1 mite allergens, especially Der p 1 and Der f 1, are major sources of house dust mite (HDM) allergies in temperate climates.[6][9][10]

  1. ^ a b Chruszcz M, Chapman MD, Vailes LD, Stura EA, Saint-Remy JM, Minor W, Pomés A (2009). "Crystal structures of mite allergens Der f 1 and Der p 1 reveal differences in surface-exposed residues that may influence antibody binding". J. Mol. Biol. 386 (2): 520–30. doi:10.1016/j.jmb.2008.12.049. PMC 2677027. PMID 19136006.
  2. ^ Meighan, P.; Pirzad, R. (2004). "Mite endopeptidase 1". In Barrett, A.J.; Rawlings, N.D.; Woessner, J.F. (eds.). Handbook of Proteolytic Enzymes (2nd ed.). London: Elsevier. pp. 1187–1189.
  3. ^ Rassam, M; Laing, WA (January 2004). "Purification and characterization of phytocystatins from kiwifruit cortex and seeds". Phytochemistry. 65 (1): 19–30. doi:10.1016/j.phytochem.2003.09.019. PMID 14697268.
  4. ^ Harris, J.; Mason, D.E.; Li, J.; Burdick, K.W.; Backes, B.J.; Chen, T.; Shipway, A.; Van Heeke, G.; Gough, L.; Ghaemmaghami, A.; Shakib, F.; Debaene, F.; Winssinger, N. (2004). "Activity profile of dust mite allergen extract using substrate libraries and functional proteomic microarrays". Chem. Biol. 11 (10): 1361–1372. doi:10.1016/j.chembiol.2004.08.008. PMID 15489163.
  5. ^ "Information on EC 3.4.22.65 - peptidase 1 (mite)". Enzyme Database - BRENDA. January 2015. Retrieved 11 April 2015.
  6. ^ a b Schulz, O.; Sewell, H.F.; Shakib, F. (1998). "A sensitive fluorescent assay for measuring the cysteine protease activity of Der p 1, a major allergen from the dust mite Dermatophagoides pteronyssinus". Mol. Pathol. 51 (4): 222–224. doi:10.1136/mp.51.4.222. PMC 395641. PMID 9893750.
  7. ^ "EURM1 - Peptidase 1 precursor - Euroglyphus maynei (Mayne's house dust mite)". UniProt. Retrieved 27 March 2015.
  8. ^ McNair, Carol M.; Billingsley, Peter F.; Nisbet, Alasdair J.; Knox, Dave P. (27 October 2009). "Feeding-associated gene expression in sheep scab mites (Psoroptes ovis)". Veterinary Research. 41 (2): 16. doi:10.1051/vetres/2009064. PMC 2789330. PMID 19852923.
  9. ^ Cui, Y.; Zhou, P.; Peng, J.; Peng, M.; Zhou, Y.; Lin, Y.; Liu, L. (May 2008). "Cloning, sequence analysis, and expression of cDNA coding for the major house dust mite allergen, Der f 1, in Escherichia coli". Brazilian Journal of Medical and Biological Research. 41 (5): 380–388. doi:10.1590/S0100-879X2008000500006. PMID 18545812.
  10. ^ Lee, AJ; Machell, J; Van Den Broek, AH; Nisbet, AJ; Miller, HR; Isaac, RE; Huntley, JF (August 2002). "Identification of an antigen from the sheep scab mite, Psoroptes ovis, homologous with house dust mite group I allergens". Parasite Immunology. 24 (8): 413–22. doi:10.1046/j.1365-3024.2002.00480.x. PMID 12406195. S2CID 37215478.