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oai:www.ideals.illinois.edu:2142/84328 2023-07-11 col_2142_5131 col_2142_14789 com_2142_5130 com_2142_14788 com_2142_8903

van der Donk, Wilfred A. Levengood, Matthew 2015-09-25T22:13:58Z 2015-09-25T22:13:58Z 10000-01-01 2008 2008 The promiscuous activity of LctM toward LctA prepeptides containing nonproteinogenic amino acids prompted the evaluation of LctM as a general catalyst for the introduction of post-translational modifications in non-lantibiotic peptides fused to the LctA leader peptide. LctM was utilized to efficiently introduce dehydrated, phosphorylated, and lanthionine cross-linked amino acids into therapeutically relevant non-lantibiotic peptides. Furthermore, enzymatically installed dehydro amino acids were used as sites of ligation with a variety of thiol nucleophiles for the preparation of peptide conjugates. Lastly, the role of the leader peptide in lacticin 481 biosynthesis was investigated. Surprisingly, the leader peptide was not required for dehydration activity of LctM, although it greatly enhanced the catalytic efficiency of LctM. Made available in DSpace on 2015-09-25T22:13:58Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3347436.pdf: 3901302 bytes, checksum: 875d6489209029c78c4c00ec37b34b40 (MD5) Previous issue date: 2008 Embargo set by: Seth Robbins for item 85609 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 250 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2008. http://hdl.handle.net/2142/84328 (MiAaPQ)AAI3347436 eng Chemistry, Biochemistry Investigations of the Substrate Specificity of Lacticin 481 Synthetase and Utilization in Peptide Engineering Applications text Chemistry Chemistry University of Illinois at Urbana-Champaign Dissertation Ph.D.