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  • Title: Site-directed mutagenesis of beta-galactosidase (E. coli) reveals that tyr-503 is essential for activity.
    Author: Ring M, Bader DE, Huber RE.
    Journal: Biochem Biophys Res Commun; 1988 May 16; 152(3):1050-5. PubMed ID: 3132151.
    Abstract:
    By using the technique of site-directed mutagenesis we have succeeded in replacing tyr-503 of beta-galactosidase (E. coli) with a phe. A study of the kinetic and stability properties of this mutant enzyme (F-503 beta-galactosidase) showed that the loss in activity upon this change is due to the loss of a catalytic group (rather than a detrimental change in the enzyme's overall structure or a change in the enzyme's binding capacity). This confirms previous suggestions that this tyr residue is involved in catalysis.
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