Investigation of the Enzymes Involved in Lantibiotic Biosynthesis: Lacticin 481 and Haloduracin

Finally, removal of the leader peptide from the modified precursor peptides is the final step in the maturation of lantibiotics, and is required for achievement of full biological activity. In lacticin 481 maturation, this peptide cleavage reaction is performed by the N-terminal protease domain of the lacticin 481 transporter, LctT. The activity of the protease domain of LctT was reconstituted in vitro and its substrate specificity was probed with numerous variants of the lacticin 481 precursor peptide. The N-terminal 150 amino acids of LctT were able to process most LctA mutant peptides, with the exception of peptides containing mutations at the double glycine motif located at the junction between leader sequence and structural region. Cys protease activity was confirmed for LctT as mutation of Cys12 to Ser or Ala abolished protease activity.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Chemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Ihnken, Leigh Anne Furgerson

Contributors dc:contributor

• van der Donk, Wilfred A.

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI3392075

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84344