Design of a glutamine substrate tag enabling protein labelling mediated by Bacillus subtilis transglutaminase.

ABSTRACT: Transglutaminases (TGases) are enzymes that catalyse protein cross-linking through a transamidation reaction between the side chain of a glutamine residue on one protein and the side chain of a lysine residue on another. Generally, TGases show low substrate specificity with respect to their amine substrate, such that a wide variety of primary amines can participate in the modification of specific glutamine residue. Although a number of different TGases have been used to mediate these bioconjugation reactions, the TGase from Bacillus subtilis (bTG) may be particularly suited to this application. It is smaller than most TGases, can be expressed in a soluble active form, and lacks the calcium dependence of its mammalian counterparts. However, little is known regarding this enzyme and its glut

SUBMITTER: Oteng-Pabi SK 

PROVIDER: S-EPMC5976192 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature