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Showing 1 to 5 of 5 for “"Procm"”.

  1. Mechanistic studies of class II lanthipeptide synthetases and yeast surface display of lanthipeptide leader peptides

    … to their diverse biological activities. ProcM is a promiscuous bifunctional synthetase that catalyzes both dehydration and cyclization of the lanthipeptides. Its 30 substrate peptides (ProcAs) have a high level of conservation in the N-terminal leader region and hypervariability in the …

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  2. Mechanistic and synthetic studies on the prochlorosin and cytolysin families of lanthipeptides

    … broad substrate scope of the synthetase ProcM inspired us to explore its mechanism in detail (chapter 2). My studies on ProcM revealed the directionality of dehydration, the order of cyclization, and that, despite the impressive substrate scope, none of the cyclizations are non-enzymatic. …

    uiuc Repository record for Mechanistic and synthetic studies on the prochlorosin and cytolysin families of lanthipeptides (opens in a new tab)

  3. Investigation and application of substrate tolerant thioether forming enzymes

    … chapter 2 using a substrate-tolerant synthetase (ProcM) from Prochlorococcus that dehydrates and cyclizes up to 30 different linear precursor peptides encoded in its genome. A bicyclic lanthipeptide library was constructed, characterized and coupled to a selection system to screen for a …

    uiuc Repository record for Investigation and application of substrate tolerant thioether forming enzymes (opens in a new tab)

  4. Mechanistic studies of lanthipeptide biosynthesis

    … by a highly substrate-tolerant synthetase ProcM in marine bacteria, is included as chapter 8. The unveiled structural information of these lanthipeptides and the biochemical studies with respect to the biosynthetic process described in this thesis may assist the genome mining and synthetic …

    uiuc Repository record for Mechanistic studies of lanthipeptide biosynthesis (opens in a new tab)

  5. Mechanistic studies of lanthipeptide biosynthetic enzymes and discovery of novel lanthipeptides

    Submission published under a 24 month embargo labeled 'Closed Access', the embargo will last until 2026-05-01

    uiuc Repository record for Mechanistic studies of lanthipeptide biosynthetic enzymes and discovery of novel lanthipeptides (opens in a new tab)