Serine protease variants having peptide ligase activity

Drug – bio-affecting and body treating compositions – Designated organic active ingredient containing – Peptide containing doai

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435 681, 435212, 435213, 435214, 435215, 435216, 435217, 435218, 435219, 435220, 435221, 435222, 435223, 435224, 435225, 435226, 530338, 530345, 530409, 530410, A61K 3800, C12P 2106, C07K 117

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active

057365121

ABSTRACT:
The invention relates to serine protease variants derived from precursor serine proteases via recombinant and/or chemical methods to form protease variants having improved peptide ligase activity. The invention also includes novel ligation substrates which in combination with the serine protease variants and a second ligation substrate are capable of forming a ligation product. The invention also relates to methods for forming such ligation products and the products formed thereby.

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Caldwell, R., et al., "Analysis of the Catalytic Importance of a Helix Dipole in Subtilisin Using Site-Directed Mutagenesis", American Chemical Society Abstract MBTD-73, Sep. 10-15, 1989.
Carter, P., et al., "Dissecting the Catalytic Triad of a Serine Protease", Nature,332 (7) :564-568 (1988).
Abrahmsen, L., et al., "Engineering Subtilisin and Its Substrates for Efficient Ligation of Peptide Bonds in Aqueous Solution", Biochemistry, 30:4151-4159 (1991).

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