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Characterization of the flavoenzyme XiaK as an N-hydroxylase and implications in indolosesquiterpene diversification
Zhang, QB; Li, HX; Yu, L; Sun, Y; Zhu, YG; Zhu, HN; Zhang, LP; Li, SM; Shen, YM; Tian, CL; Li, A; Liu, HW; Zhang, CS;;
Source PublicationCHEMICAL SCIENCE
AbstractFlavoenzymes are ubiquitous in biological systems and catalyze a diverse range of chemical transformations. The flavoenzyme XiaK from the biosynthetic pathway of the indolosesquiterpene xiamycin A is demonstrated to mediate the in vivo biotransformation of xiamycin A into multiple products, including a chlorinated adduct as well as dimers characterized by C-N and N-N linkages that are hypothesized to form via radical-based mechanisms. Isolation and characterization of XiaK in vitro shows that it acts as a flavin-dependent N-hydroxylase that catalyzes the hydroxylation of xiamycin A at the carbazole nitrogen to form N-hydroxyxiamycin, a product which was overlooked in earlier in vivo experiments because its chemical and chromatographic properties are similar to those of oxiamycin. N-Hydroxyxiamycin is shown to be unstable under aerobic conditions, and characterization by electron paramagnetic resonance spectroscopy demonstrates formation of an N-hydroxycarbazole radical adduct. This radical species is proposed to serve as a key intermediate leading to the formation of the multiple xiamycin A adducts. This study suggests that non-enzyme catalyzed reactions may play a greater role in the biosynthesis of natural products than has been previously recognized.
Department[Zhang, Qingbo; Li, Huixian; Zhu, Yiguang; Zhu, Hanning; Zhang, Liping; Zhang, Changsheng] Chinese Acad Sci, CAS Key Lab Trop Marine Bioresources & Ecol, Guangdong Key Lab Marine Mat Med, South China Sea Inst Oceanol, 164 West Xingang Rd, Guangzhou 510301, Guangdong, Peoples R China; [Li, Huixian] Sun Yat Sen Univ, South China Sea Resource Exploitat & Protect Coll, Sch Marine Sci, Inst Marine Nat Prod, 135 West Xingang Rd, Guangzhou 510006, Guangdong, Peoples R China; [Yu, Lu; Tian, Changlin; Li, Ang] Univ Sci & Technol China, Sch Life Sci, Hefei Natl Lab Microscale Phys Sci, Hefei 230027, Peoples R China; [Yu, Lu] Chinese Acad Sci, High Magnet Field Lab, Hefei 230031, Peoples R China; [Sun, Yu] Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, 345 Lingling Rd, Shanghai 200032, Peoples R China; [Li, Shu-Ming] Philipps Univ Marburg, Inst Pharmazeut Biol & Biotechnol, Deutschhausstr 17a, D-35037 Marburg, Germany; [Shen, Yuemao] Shandong Univ, Sch Life Sci, State Key Lab Microbial Technol, Jinan 250100, Peoples R China; [Liu, Hung-Wen] Univ Texas Austin, Dept Chem, Coll Pharm, Div Chem Biol & Med Chem, Austin, TX 78712 USA
Funding ProjectLMB
Document Type期刊论文
Recommended Citation
GB/T 7714
Zhang, QB,Li, HX,Yu, L,et al. Characterization of the flavoenzyme XiaK as an N-hydroxylase and implications in indolosesquiterpene diversification[J]. CHEMICAL SCIENCE,2017,8(7):5067-5077.
APA Zhang, QB.,Li, HX.,Yu, L.,Sun, Y.,Zhu, YG.,...& of the flavoenzyme XiaK as an N-hydroxylase and implications in indolosesquiterpene diversification.CHEMICAL SCIENCE,8(7),5067-5077.
MLA Zhang, QB,et al."Characterization of the flavoenzyme XiaK as an N-hydroxylase and implications in indolosesquiterpene diversification".CHEMICAL SCIENCE 8.7(2017):5067-5077.
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