Deciphering the Origin and Formation of Aminopyrrole Moiety in Kosinostatin Biosynthesis,Chinese Journal of Chemistry

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Deciphering the Origin and Formation of Aminopyrrole Moiety in Kosinostatin Biosynthesis
Chinese Journal of Chemistry ( IF 5.5 ) Pub Date : 2021-09-01 , DOI: 10.1002/cjoc.202100525
Yu Hu ₁ , Qiang Zhou _{1,

2} , Zhuan Zhang ₁ , Hai‐Xue Pan _{1,

3} , Yulia Ilina ₄ , Mikko Metsä‐Ketelä ₄ , Yasuhiro Igarashi ₅ , Gong‐Li Tang _{1,

3}

Affiliation

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.

中文翻译：

破译 Kosinostatin 生物合成中氨基吡咯部分的起源和形成

Kosinostatin (KST) 包含一个罕见的氨基吡咯部分，其生物合成仍然难以捉摸。在此，由 L-四氢嘧啶合酶样酶 KstB3 通过 L-谷氨酰胺环化产生的氨基吡咯啉酸被鉴定为腺苷酸化酶 KstB1 的真正底物。随后，FAD 依赖性脱氢酶 KstB4 和转谷氨酰胺酶样酶 KstB6 也参与了氨基吡咯的形成。这些结果为 KST 生物合成中 2-氨基吡咯的形成提供了一条不寻常的途径。

更新日期：2021-09-01

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