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Functional implication of disulfide bond, Cys250 -Cys283, in bovine chymosin.

Huang K., Zhang Z., Liu N., Zhang Y., Zhang G., Yang K.

The reduction, carboxymethylation and mercuration of disulfide bond, Cys250-Cys283, located on the surface of bovine chymosin molecule resulted in the loss of about 25% of enzyme activity, suggesting that Cys250-Cys283 is not intimately involved in catalytic mechanism. Cys250 and Cys283 were substituted with Asp. and Ser. by site-directed mutagenesis of the structural gene coding for bovine prochymosin B. All three mutants (C250D/C283S, C250D, C283S) failed to be activated to chymosin in acid, indicating that Cys250-Cys283 might have some contribution to the correct refolding of the unfolded prochymosin.

Biochem. Biophys. Res. Commun. 187:692-696(1992) [PubMed] [Europe PMC]

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