Specificity stringency: Prime-low, Nonprime-low, only stringent to the C-terminal active ester/thioester served as a leaving group
Expression Platform:
E. coli
Mutations:
Protease-to-ligase conversion of subtilisin BPN': S221C/P225A
Other Properties:
-
References:
[1]
(Discovery) Abrahmsén, L.; Tom, J.; Burnier, J.; Butcher, K. A.; Kossiakoff, A.; Wells, J. A. Engineering subtilisin and its substrates for efficient ligation of peptide bonds in aqueous solution. Biochemistry 1991, 30 (17), 4151-4159.
DOI: 10.1021/bi00231a007
[2]
(Sequence, Activity) Chang, T. K.; Jackson, D. Y.; Burnier, J. P.; Wells, J. A. Subtiligase: a tool for semisynthesis of proteins. Proceedings of the National Academy of Sciences 1994, 91 (26), 12544-12548.
DOI: 10.1073/pnas.91.26.12544
[3]
(Application) Braisted, A. C.; Judice, J. K.; Wells, J. A. Synthesis of proteins by subtiligase. Methods Enzymol 1997, 289, 298-313.
DOI: 10.1016/s0076-6879(97)89053-2