Discovery of the Biosynthetic Pathway of Beticolin 1 Reveals a Novel Non‐Heme Iron‐Dependent Oxygenase for Anthraquinone Ring Cleavage. (4th August 2022)

• Record Type: Journal Article
• Authors: Hou, Xiaodong; Xu, Huibin; Deng, Zhiwei; Yan, Yijun; Yuan, Zhenbo; Liu, Xuanzhong; Su, Zengping; Yang, Sai; Zhang, Yan; Rao, Yijian
• Is Part Of: Angewandte Chemie. Volume 134:Number 37(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-08-04
• Subjects: Anthraquinone Ring Cleavage -- Beticolin 1 -- Biosynthetic Gene Cluster -- Carboxylated-Lysine -- Non-Heme Iron Oxygenase; Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.202208772
• Languages: English
• ISSNs: 0044-8249

Abstract

Abstract: This study used light‐mediated comparative transcriptomics to identify the biosynthetic gene cluster of beticolin 1 in Cercospora . It contains an anthraquinone moiety and an unusual halogenated xanthone moiety connected by a bicyclo[3.2.2]nonane. During elucidation of the biosynthetic pathway of beticolin 1, a novel non‐heme iron oxygenase BTG13 responsible for anthraquinone ring cleavage was discovered. More importantly, the discovery of non‐heme iron oxygenase BTG13 is well supported by experimental evidence: (i) crystal structure and the inductively coupled plasma mass spectrometry revealed that its reactive site is built by an atypical iron ion coordination, where the iron ion is uncommonly coordinated by four histidine residues, an unusual carboxylated‐lysine (Kcx377) and water; (ii) Kcx377 is mediated by His58 and Thr299 to modulate the catalytic activity of BTG13. Therefore, we believed this study updates our knowledge of metalloenzymes. Abstract : A novel non‐heme iron oxygenase BTG13 required for anthraquinone ring cleavage is discovered during elucidation of the biosynthetic pathway of beticolin 1, in which iron is uncommonly coordinated by four histidine residues, an unusual carboxylated‐lysine (Kcx377) and water based on its crystal structure. Moreover, Thr299 and His58 mediate Kcx377 to modulate the catalytic activity of BTG13. Thus, this work updates our knowledge of metalloenzymes.