Protein having prolyl oligopeptidase activity, and...

Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase

Reexamination Certificate

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Reexamination Certificate

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07741094

ABSTRACT:
A protein of amino acid sequence SEQ ID NO:6 isolated fromCoprinus clastophyllus. The protein is stable at 30 to 37 degrees centigrade and has an optimal prolyl oligopeptidase activity at about 45 degree centigrade and at about pH 7. The present invention also relates to a medicament comprising such protein for treating celiac disease caused by proline abundant gluten.

REFERENCES:
Galye et al, Identification of regions in interleukin-1 alpha important for activity. J Biol Chem. Oct. 15, 1993;268(29):22105-11.
Whisstock et al, Prediction of protein function from protein sequence and structure. Q Rev Biophys. Aug. 2003;36(3):307-40. Review.
Marti et al, Prolyl endopeptidase-mediated destruction of T cell epitopes in whole gluten: chemical and immunological characterization. J Pharmacol Exp Ther. Jan. 2005;312(1):19-26. Epub Sep. 9, 2004.
Piper et al, Effect of prolyl endopeptidase on digestive-resistant gliadin peptides in vivo. J Pharmacol Exp Ther. Oct. 2004;311(1):213-9. Epub May 13, 2004.
Gass et al, Fermentation, purification, formulation, and pharmacological evaluation of a prolyl endopeptidase fromMyxococcus xanthus: implications for Celiac Sprue therapy. Biotechnol Bioeng. Dec. 20, 2005;92(6):674-84.
Matysiak-Budnik et al, Limited efficiency of prolyl-endopeptidase in the detoxification of gliadin peptides in celiac disease. Gastroenterology. Sep. 2005;129(3):786-96.
Pyle et al, Effect of Pretreatment of Food Gluten With Prolyl Endopeptidase on Gluten-Induced Malabsorption in Celiac Sprue Clinical Gastroenterology and Hepatology, (2005) vol. 3, Issue 7, pp. 687-694.

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