Engineering proteases with altered specificity

Jonathan P. Leis*, Craig E. Cameron

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


Recent analysis of the crystal structures, both of the retroviral aspartyl proteases from Rous sarcoma virus and human immunodeficiency virus type 1 and of the serine proteases subtilisin and α-lytic protease, has enabled the rational design of mutations in the substrate-binding pocket of these enzymes. Alterations in steady-state kinetic properties of the purified mutant enzymes have been detected in vitro by following the cleavage of synthetic peptide substrates. These analyses have identified key amino acid residues in each of these enzymes that are involved in substrate specificity, and they have provided the foundation for the design of proteases with novel substrate specificities.

Original languageEnglish (US)
Pages (from-to)403-408
Number of pages6
JournalCurrent Opinion in Biotechnology
Issue number4
StatePublished - Aug 1994

ASJC Scopus subject areas

  • Bioengineering
  • Biotechnology
  • Biomedical Engineering


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