Investigation of the Enzymes Involved in Lantibiotic Biosynthesis: Lacticin 481 and Haloduracin
Ihnken, Leigh Anne Furgerson
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https://hdl.handle.net/2142/84344
Description
Title
Investigation of the Enzymes Involved in Lantibiotic Biosynthesis: Lacticin 481 and Haloduracin
Author(s)
Ihnken, Leigh Anne Furgerson
Issue Date
2009
Doctoral Committee Chair(s)
van der Donk, Wilfred A.
Department of Study
Chemistry
Discipline
Chemistry
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Chemistry, Biochemistry
Language
eng
Abstract
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.
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