Design and efficient production of bovine enterokinase light chain with higher specificity in E. coli
- Authors
- Chun, Haarin; Joo, Keehyoung; Lee, Jooyoung; Shin, Hang-Cheol
- Issue Date
- Jun-2011
- Publisher
- SPRINGER
- Keywords
- Enterokinase; Fusion protein; Protein disulfide isomerase; Mutants
- Citation
- BIOTECHNOLOGY LETTERS, v.33, no.6, pp.1227 - 1232
- Journal Title
- BIOTECHNOLOGY LETTERS
- Volume
- 33
- Number
- 6
- Start Page
- 1227
- End Page
- 1232
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/13655
- DOI
- 10.1007/s10529-011-0562-3
- ISSN
- 0141-5492
- Abstract
- Enterokinase light chain (EKL) is a serine protease that recognizes Asp-Asp-Asp-Asp-Lys (D(4)K) sequence and cleaves the C-terminal peptide bond of the lysine residue. The utility of EKL as a site-specific cleavage enzyme is hampered by sporadic cleavage at other sites than the canonical D4K recognition sequence. In order to produce more site-specific EKL, we have generated several EKL mutants in E. coli with substitutions at Tyr174 and Lys99 using PDI (protein disulfide isomerase) fusion system. Substitution of Tyr174 by basic residues confers higher specificity on EKL. The production of EKL with higher specificity could widen the utility of EKL as a site-specific cleavage enzyme to produce various recombinant proteins with therapeutic or industrial values.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - College of Natural Sciences > School of Systems and Biomedical Science > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/13655)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.