TY - JOUR
T1 - Elucidation of the roles of conserved residues in the biosynthesis of the lasso peptide paeninodin
AU - Hegemann, Julian D.
AU - Schwalen, Christopher J.
AU - Mitchell, Douglas A.
AU - Van der Donk, Wilfred A.
N1 - Funding Information:
This work was supported by grants from the Howard Hughes Medical Institute (to W. A. V.), the David and Lucile Packard Fellowship for Science and Engineering (to D. A. M.), the Deutsche Forschungsgemeinschaft (DFG Research Fellowship 309199717 to J. D. H.), and the Chemistry-Biology Interface Training Program (GM070421 to C. J. S.). A Bruker UltrafleXtreme MALDI TOF/TOF mass spectrometer was bought in part with a grant from the National Institutes of Health (S10 RR027109 A). We thank Prof. Mohamed Marahiel for providing some of the plasmids used in this study.
Publisher Copyright:
© The Royal Society of Chemistry.
PY - 2018
Y1 - 2018
N2 - Substrate binding assays, in vitro proteolytic processing assays, and heterologous lasso peptide production were used to investigate the roles of conserved precursor peptide residues during paeninodin maturation. Specifically, we delineate which residues are important for substrate recognition, proteolysis, and lasso peptide macrocyclization.
AB - Substrate binding assays, in vitro proteolytic processing assays, and heterologous lasso peptide production were used to investigate the roles of conserved precursor peptide residues during paeninodin maturation. Specifically, we delineate which residues are important for substrate recognition, proteolysis, and lasso peptide macrocyclization.
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U2 - 10.1039/c8cc04411b
DO - 10.1039/c8cc04411b
M3 - Article
C2 - 30046789
AN - SCOPUS:85051482974
SN - 1359-7345
VL - 54
SP - 9007
EP - 9010
JO - Chemical Communications
JF - Chemical Communications
IS - 65
ER -