Variants of the industrially relevant protease KP-43 with suppressed activity under alkaline conditions developed using expanded genetic codes
Open Access
- 12 December 2018
- journal article
- research article
- Published by Elsevier in Biochemistry and Biophysics Reports
- Vol. 17, 93-96
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- A single mutation within a Ca2+ binding loop increases proteolytic activity, thermal stability, and surfactant stabilityBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2013
- Genetic-code evolution for protein synthesis with non-natural amino acidsBiochemical and Biophysical Research Communications, 2011
- Codon reassignment in the Escherichia coli genetic codeNucleic Acids Research, 2010
- Detergent alkaline proteases: enzymatic properties, genes, and crystal structuresJournal of Bioscience and Bioengineering, 2007
- The Crystal Structure of an Oxidatively Stable Subtilisin-like Alkaline Serine Protease, KP-43, with a C-terminal β-Barrel DomainJournal of Biological Chemistry, 2004
- Rational engineering of enzyme stabilityJournal of Biotechnology, 2004
- Detergent proteasesCurrent Opinion in Biotechnology, 2004
- Bacterial alkaline proteases: molecular approaches and industrial applicationsApplied Microbiology and Biotechnology, 2002
- A novel species of alkaliphilic Bacillus that produces an oxidatively stable alkaline serine proteaseExtremophiles, 2002
- STRUCTURAL AND GENETIC ANALYSIS OF PROTEIN STABILITYAnnual Review of Biochemistry, 1993