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Takai, T, Kato, T, Sakata, Y, Yasueda, H, Izuhara, K, Okumura, K and Ogawa, H (2005) Recombinant Der p 1 and Der f 1 exhibit cysteine protease activity but no serine protease activity. Biochem. Biophys. Res. Commun. 328:944-52
Although mite major group 1 allergens, Der p 1 and Der f 1, were first isolated as cysteine proteases, some studies reported that natural Der p 1 exhibits mixed cysteine and serine protease activity. Clarifying whether the serine protease activity originates from Der p 1 or is due to contamination is important for distinguishing between the pathogenic proteolytic activities of group 1 allergens and mite-derived serine proteases. Recombinant mite group 1 allergens would be useful tool for addressing this issue, because they are completely free from contamination by mite serine proteases. Recombinant Der p 1 and Der f 1, and highly purified natural forms exhibited only cysteine protease activity. However, commercially available natural forms exhibited both activities, but the two activities were eluted into different fractions in size-exclusion column chromatography. The substrate specificity associated with the serine protease activity was similar to that of Der f 3. These results indicate that the serine protease activity does not originate from group 1 allergens.
Antigens, Dermatophagoides/chemistry; Antigens, Dermatophagoides/genetics; Arthropod Proteins; Cysteine Endopeptidases/chemistry; Enzyme Activation; Kinetics; Pichia/enzymology; Pichia/genetics; Pyroglyphidae/enzymology; Pyroglyphidae/genetics; Recombinant Proteins/chemistry; Serine Endopeptidases/chemistry; Substrate Specificity
|Gene product||Qualifier||GO Term||Evidence Code||with/from||Aspect||Extension||Notes||Status|
|GO:0008234: cysteine-type peptidase activity||
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