Design of highly active substrates using molecular docking for microbial transglutaminase detection.

ABSTRACT: The transglutaminase (TGase) family catalyzes a transamidation reaction between glutamine (Gln) and lysine (Lys) residues on protein substrates. Highly active substrates are important for cross-linking and modifying proteins of TGase. In the present work, high-activity substrates have been designed based on the principles of enzyme-substrate interaction, using microbial transglutaminase (mTGase) as a research model of the TGase family. Substrates with high activity were screened using a combination of molecular docking and traditional experiments. Twenty-four sets of peptide substrates all produced good catalytic activity with mTGase. FFKKAYAV as the acyl acceptor and VLQRAY as the acyl donor group had the best reaction efficiency with highly sensitive detection of 26 nM mTGase. In additio

SUBMITTER: Zou L 

PROVIDER: S-EPMC9923216 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature