A naturally variable residue in the S1 subsite of M1 family aminopeptidases modulates catalytic properties and promotes functional specialization

Abstract

Background: M1 family aminopeptidases exhibit a diverse range of specificities. Results: Substitutions at a residue in the S1 binding pocket can induce structural changes and remodel specificity. Conclusion: Mutations in the S1 subsite contribute to the acquisition of distinct specificities. Significance: Variation of a key residue in the S1 binding pocket provides a pathway for the evolution of new specificities and functions. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.