Ontology highlight
ABSTRACT:
SUBMITTER: Fiebig D
PROVIDER: S-EPMC5034039 | biostudies-literature | 2016 Sep
REPOSITORIES: biostudies-literature
Fiebig David D Schmelz Stefan S Zindel Stephan S Ehret Vera V Beck Jan J Ebenig Aileen A Ehret Marina M Fröls Sabrina S Pfeifer Felicitas F Kolmar Harald H Fuchsbauer Hans-Lothar HL Scrima Andrea A
The Journal of biological chemistry 20160804 39
Transglutaminase from Streptomyces mobaraensis (MTG) is an important enzyme for cross-linking and modifying proteins. An intrinsic substrate of MTG is the dispase autolysis-inducing protein (DAIP). The amino acid sequence of DAIP contains 5 potential glutamines and 10 lysines for MTG-mediated cross-linking. The aim of the study was to determine the structure and glutamine cross-linking sites of the first physiological MTG substrate. A production procedure was established in Escherichia coli BL21 ...[more]