doi: 10.1016/s0006-291x(88)80390-5.
Site-directed mutagenesis of beta-galactosidase (E. coli) reveals that tyr-503 is essential for activity
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- PMID: 3132151
- DOI: 10.1016/s0006-291x(88)80390-5
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Site-directed mutagenesis of beta-galactosidase (E. coli) reveals that tyr-503 is essential for activity
Biochem Biophys Res Commun.
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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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