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oai:www.ideals.illinois.edu:2142/84344 2023-07-11 col_2142_5131 col_2142_14789 com_2142_5130 com_2142_14788 com_2142_8903

van der Donk, Wilfred A. Ihnken, Leigh Anne Furgerson 2015-09-25T22:14:02Z 2015-09-25T22:14:02Z 10000-01-01 2009 2009 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. Made available in DSpace on 2015-09-25T22:14:02Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3392075.pdf: 2113071 bytes, checksum: 22edbc2920de44980bb902dcc2c02494 (MD5) Previous issue date: 2009 Embargo set by: Seth Robbins for item 85625 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 140 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2009. http://hdl.handle.net/2142/84344 (MiAaPQ)AAI3392075 eng Chemistry, Biochemistry Investigation of the Enzymes Involved in Lantibiotic Biosynthesis: Lacticin 481 and Haloduracin text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.