Article
Structure mediation in substrate binding and post-translational processing of penicillin acylases: Information from mutant structures of Kluyvera citrophila penicillin G acylase.
Protein science : a publication of the Protein Society - 1 Oct 2015
Chand Deepak, Varshney NishantKumar, Ramasamy Sureshkumar, Panigrahi Priyabrata, Brannigan James A, Wilkinson Anthony J, Suresh C G
Abstract excerpt
Penicillin acylases are industrially important enzymes for the production of 6-APA, which is used extensively in the synthesis of secondary antibiotics. The enzyme translates into an inactive single chain precursor that subsequently gets processed by the removal of a spacer peptide connecting the chains of the mature active heterodimer. We have cloned the penicillin G acylase from Kluyvera citrophila (KcPGA) and...
Topics
- Binding Sites
- Crystallography, X-Ray
- Kluyvera
- Molecular Conformation
- Mutagenesis, Site-Directed
- Mutation
- Penicillin Amidase
- Protein Binding
- Protein Processing, Post-Translational
- Quorum Sensing
- Structure-Activity Relationship
- Substrate Specificity