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机构地区:[1]Graduate School of Pharmaceutical Sciences,The University of Tokyo,Tokyo,Japan [2]Collaborative Research Institute for Innovative Microbiology,The University of Tokyo,Tokyo,Japan
出 处:《Engineering Microbiology》2023年第1期56-64,共9页工程微生物学(英文)
基 金:supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education,Culture,Sports,Science and Technology,Japan(JSPS KAKENHI Grant No.JP16H06443,JP20KK013,and JP20H00490);Japan Science and Technology Agency(JST SICORP Grant No.JPMJSC1701);the New Energy and Industrial Technology Development Organization(NEDO,Grant No.JPNP20011);Japan Agency for Medical Research and Development(AMED)(Grant No.JP21ak0101164);H.T.is a recipient of the JSPS Postdoctoral Fellowship for Foreign Researchers(ID No.P18404).
摘 要:Fe(Ⅱ)/α-ketoglutarate(αKG)-dependent oxygenases catalyze the oxidative modification of various molecules,from DNA,RNA,and proteins to primary and secondary metabolites.They also catalyze a variety of biochemical reactions,including hydroxylation,halogenation,desaturation,epoxidation,cyclization,peroxidation,epimeriza-tion,and rearrangement.Given the versatile catalytic capability of such oxygenases,numerous studies have been conducted to characterize their functions and elucidate their structure-function relationships over the past few decades.Amino acids,particularly nonproteinogenic amino acids,are considered as important building blocks for chemical synthesis and components for natural product biosynthesis.In addition,the Fe(Ⅱ)/αKG-dependent oxy-genase superfamily includes important enzymes for generating amino acid derivatives,as they efficiently modify various free-standing amino acids.The recent discovery of new Fe(Ⅱ)/αKG-dependent oxygenases and the repur-posing of known enzymes in this superfamily have promoted the generation of useful amino acid derivatives.Therefore,this study will focus on the recent progress achieved from 2019 to 2022 to provide a clear view of the mechanism by which these enzymes have expanded the repertoire of free amino acid oxidative modifications.
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