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Literature summary for 3.4.21.81 extracted from

  • Hemmi, H.; Kumazaki, T.; Kojima, S.; Yoshida, T.; Ohkubo, T.; Yokosawa, H.; Miura, K.; Kobayashi, Y.
    Increasing the hydrolysis constant of the reactive site upon introduction of an engineered Cys14-Cys39 bond into the ovomucoid third domain from silver pheasant (2011), J. Pept. Sci., 17, 595-600.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
additional information introduction of site-specific disulfide bonds into the flexible N-terminal loop of natural Kazal-type inhibitors to characterize the thermodynamics of the reactive site peptide bond hydrolysis. Mutant P14C/N39C is a disulfide variant of the ovomucoid third domain from silver pheasant carrying an engineered Cys14–Cys39 bond near the reactive site. The conversion rate of P14C/N39C by streptogrisin B is much faster than that for wild type under any pH condition Streptomyces griseus

Organism

Organism UniProt Comment Textmining
Streptomyces griseus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
OMSVP3 + H2O ovomucoid third domain from silver pheasant, potent inhibitor of chymotrypsin, subtilisin, and elastase Streptomyces griseus ? cleavage between residues Met18-Glu19 ?
OMSVP3 mutant P14C/N39C + H2O disulfide variant of the ovomucoid third domain from silver pheasant carrying an engineered Cys14-Cys39 bond near the reactive site Streptomyces griseus ? cleavage between residues Met18-Glu19. P14C/N39C can be selectively cleaved by Streptomyces griseus protease B at the reactive site of OMSVP3 to form a reactive site modified inhibitor. The conversion rate of P14C/N39C is much faster than that for wild type under any pH condition. The reactive site modified form of P14C/N39C is thermodynamically more stable than the intact one ?