Deciphering the Origin and Formation of Aminopyrrole Moiety in Kosinostatin Biosynthesis

Abstract

Main observation and conclusion Kosinostatin (KST) contains an uncommon aminopyrrole moiety, whose biosynthesis has remained elusive. Herein, aminopyrrolinic acid, which was generated by an L‐ectoine synthase‐like enzyme KstB3 via cyclization of L‐glutamine, was identified to be the real substrate of adenylation enzyme KstB1. Subsequently, a FAD‐dependent dehydrogenase KstB4 along with a transglutaminase‐like enzyme KstB6 were also involved in formation of aminopyrrole. These results provided an unusual pathway for 2‐aminopyrrole formation in KST biosynthesis.

Characterizing Post‐PKS Modifications of 16‐Demethyl‐rifamycin Revealed Two Dehydrogenases Diverting the Aromatization Mode of Naphthalenic Ring in Ansamycin Biosynthesis

“…TP‐A0468 (M‐ rif , Figure 1A) in our biosynthetic study of kosinostatin. [ 8‐9 ] The biosynthesis of 16‐demethyl‐ rifamycins in Micromonospora sp. TP‐A0468 was investigated to verify rifamycin biosynthetic pathway and seek answers for undetermined questions.…”