Intein-VMA1 - Peptide Ligase Database

Host Organism

Saccharomyces cerevisiae

Type

Intein

Sequence

MVTGEENVYLKSSLSILKELSLDELLNVQYDVTTLIAKRVQALQNRNKCVLEEPNSKLAEILCHEKNAPQQSSQTSAGPGEQDSEDFILTQFDEDIKKESAEVHYRNENKHTVQLPLVTMPPNRHKRKISEFSSPLNGLNNLSDLEDCSDTVIHEKDNDKENKTRKLLGIELENPESTSPNLYKNVKDNFLFDFNTNPLTKRAWILEDFRPNEDIAPVKRGRRKLERFYAQVGKPEDSKHRSLSVVIESQNSDYEFAFDNLRNRSKSPPGFGRLDFPSTQEGNEDKKKSQEIIRRKTKYRFLMASNNKIPPYEREYVFKREQLNQIVDDGCFFWSDKLLQIYARC

External Links

PDB ID: -

EC: -

MEROPS: -

UniProt ID: -

NCBI: -

Substrate Specificity

P1'

Cys/Thr/Ser

Functions

Intermolecular backbone terminal ligation
Backbone terminal cyclization
C-terminal thioester formation
Specificity stringency: Prime-low, Nonprime-low, only stringent to the P1"-Cys

Expression Platform:

E. coli

Mutations:

Other Properties:

References:

[1] (Discovery) Davis, E. O.; Jenner, P. J.; Brooks, P. C.; Colston, M. J.; Sedgwick, S. G. Protein splicing in the maturation of M. tuberculosis recA protein: a mechanism for tolerating a novel class of intervening sequence. Cell 1992, 71 (2), 201-210. DOI: 10.1016/0092-8674(92)90349-h
[2] (Nomenclature) Perler, F. B.; Davis, E. O.; Dean, G. E.; Gimble, F. S.; Jack, W. E.; Neff, N.; Noren, C. J.; Thorner, J.; Belfort, M. Protein splicing elements: inteins and exteins — a definition of terms and recommended nomenclature. Nucleic Acids Research 1994, 22 (7), 1125-1127. DOI: https://doi.org/10.1093/nar/22.7.1125
[3] (Mechanism) Chong, S.; Xu, M.-Q. Protein Splicing of the Saccharomyces cerevisiae VMA Intein without the Endonuclease Motifs. Journal of Biological Chemistry 1997, 272 (25), 15587-15590. DOI: https://doi.org/10.1074/jbc.272.25.15587
[4] (Application) Xu, M. Q.; Evans, T. C., Jr. Intein-mediated ligation and cyclization of expressed proteins. Methods 2001, 24 (3), 257-277. DOI: 10.1006/meth.2001.1187