Abstract
The substrate specificity of α-lytic protease has been changed dramatically, with a concomitant increase in activity, by replacing an active-site Met with Ala. The substrate specificity of both this mutant and another similar mutant are extraordinarily broad. X-ray crystallographic analysis shows that structural plasticity, a combination of alternate side-chain conformations and binding-site flexibility, allows both large and small substrates to be well accommodated.
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Bone, R., Silen, J. & Agard, D. Structural plasticity broadens the specificity of an engineered protease. Nature 339, 191–195 (1989). https://doi.org/10.1038/339191a0
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DOI: https://doi.org/10.1038/339191a0
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