TY - JOUR
T1 - Radical SAM Enzyme QmpB Installs Two 9-Membered Ring Sactionine Macrocycles during Biogenesis of a Ribosomal Peptide Natural Product
AU - Caruso, Alessio
AU - Seyedsayamdost, Mohammad R.
N1 - Publisher Copyright:
© 2021 American Chemical Society.
PY - 2021/8/20
Y1 - 2021/8/20
N2 - We report the reaction catalyzed by QmpB, a new radical S-adenosylmethionine enzyme encoded by a ribosomal peptide natural product gene cluster in Streptococcus suis. Using isotopic labeling, site-directed mutagenesis, high-resolution mass spectrometry, and multidimensional NMR spectroscopy, we show that QmpB installs two 9-membered ring sactionine bridges, connecting a Cys residue with an upstream Asn via an α-thioether bridge, with the two macrocycles separated by a single residue. QmpB is only the second type II sactionine synthase characterized to date.
AB - We report the reaction catalyzed by QmpB, a new radical S-adenosylmethionine enzyme encoded by a ribosomal peptide natural product gene cluster in Streptococcus suis. Using isotopic labeling, site-directed mutagenesis, high-resolution mass spectrometry, and multidimensional NMR spectroscopy, we show that QmpB installs two 9-membered ring sactionine bridges, connecting a Cys residue with an upstream Asn via an α-thioether bridge, with the two macrocycles separated by a single residue. QmpB is only the second type II sactionine synthase characterized to date.
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U2 - 10.1021/acs.joc.1c01507
DO - 10.1021/acs.joc.1c01507
M3 - Article
C2 - 34351169
AN - SCOPUS:85113847422
SN - 0022-3263
VL - 86
SP - 11284
EP - 11289
JO - Journal of Organic Chemistry
JF - Journal of Organic Chemistry
IS - 16
ER -