文献类型：期刊文献

英文题名：Recent examples of -ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses

作者：Gao, Shu-Shan[1];Naowarojna, Nathchar[2];Cheng, Ronghai[2];Liu, Xueting[2,3];Liu, Pinghua[2]

机构：[1]Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing 100101, Peoples R China;[2]Boston Univ, Dept Chem, 590 Commonwealth Ave, Boston, MA 02215 USA;[3]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2018

卷号：35

期号：8

起止页码：792

外文期刊名：NATURAL PRODUCT REPORTS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000442614600006)】；

基金：Some of the work covered here is supported in part by grants from the National Institutes of Health (R01 GM093903) and the National Science Foundation (CHE-1309148) to P. L., and by a grant from the National Natural Science Foundation of China (81573341 and 31720103901) to X. L. X. L. is supported by a fellowship from Chinese Scholarship Council.

语种：英文

摘要：Covering: up to 2018-Ketoglutarate (KG, also known as 2-oxoglutarate)-dependent mononuclear non-haem iron (KG-NHFe) enzymes catalyze a wide range of biochemical reactions, including hydroxylation, ring fragmentation, C-C bond cleavage, epimerization, desaturation, endoperoxidation and heterocycle formation. These enzymes utilize iron(ii) as the metallo-cofactor and KG as the co-substrate. Herein, we summarize several novel KG-NHFe enzymes involved in natural product biosyntheses discovered in recent years, including halogenation reactions, amino acid modifications and tailoring reactions in the biosynthesis of terpenes, lipids, fatty acids and phosphonates. We also conducted a survey of the currently available structures of KG-NHFe enzymes, in which KG binds to the metallo-centre bidentately through either a proximal- or distal-type binding mode. Future structure-function and structure-reactivity relationship investigations will provide crucial information regarding how activities in this large class of enzymes have been fine-tuned in nature.