A New Member of the 4-Methylideneimidazole-5-one-containing Aminomutase Family from the Enediyne Kedarcidin Biosynthetic Pathway

CORC > 昆明植物研究所 > 中国科学院昆明植物研究所 > 植物化学与西部植物资源持续利用国家重点实验室

	A New Member of the 4-Methylideneimidazole-5-one-containing Aminomutase Family from the Enediyne Kedarcidin Biosynthetic Pathway
	Huang Sheng-Xiong ; Lohman Jeremy R. ; Huang Tingting ; Shen Ben*
刊名	Proc. Natl. Acad. Sci. USA
	2013
期号	110 页码:8069-8074
英文摘要	4-Methylideneimidazole-5-one (MIO)-containing aminomutases catalyze the conversion of L-α-amino acids to β-amino acids with either an (R) or an (S) configuration. L Phenylalanine and L-tyrosine are the only two natural substrates identified to date. The enediyne chromophore of the chromoprotein antitumor antibiotic kedarcidin (KED)harbors an (R)-2-aza-3-chloro-β-tyrosine moiety reminiscent of the (S)-3-chloro-5-hydroxy-β-tyrosine moiety of the C-1027 enediyne chromophore, the biosynthesis of which uncovered the first known MIO-containing aminomutase, SgcC4. Comparative analysis of the KED and C-1027 biosynthetic gene clusters inspired the proposal for (R)-2-aza-3 chloro-β-tyrosine biosynthesis starting from 2-aza-L-tyrosine, featuring KedY4 as a putative MIO-containing aminomutase. Here we report the biochemical characterization of KedY4, confirming its proposed role in KED biosynthesis. KedY4 is anMIO-containing aminomutase that stereospecifically catalyzes the conversion of 2-aza-L-tyrosine to (R)-2-aza-β-tyrosine, exhibiting no detectable activity toward 2-aza-L-phenylalanine or L-tyrosine as an alternative substrate. In contrast, SgcC4, which stereospecifically catalyzes the conversion of L-tyrosine to (S)-β-tyrosine in C-1027 biosynthesis, exhibits minimal activity with 2-aza-L-tyrosine as an alternative substrate but generating (S)-2-aza-β-tyrosine, a product with the opposite stereochemistry of KedY4. This report of KedY4 broadens the scope of known substrates for the MIO-containing aminomutase family, and comparative studies of KedY4 and SgcC4 provide an outstanding opportunity to examine how MIO-containing aminomutases control substrate specificity and product enantioselectivity.
收录类别	SCI
公开日期	2014-04-16
内容类型	期刊论文
源URL	[http://ir.kib.ac.cn/handle/151853/18017]
专题	昆明植物研究所_植物化学与西部植物资源持续利用国家重点实验室
推荐引用方式 GB/T 7714	Huang Sheng-Xiong,Lohman Jeremy R.,Huang Tingting,et al. A New Member of the 4-Methylideneimidazole-5-one-containing Aminomutase Family from the Enediyne Kedarcidin Biosynthetic Pathway[J]. Proc. Natl. Acad. Sci. USA,2013(110):8069-8074.
APA	Huang Sheng-Xiong,Lohman Jeremy R.,Huang Tingting,&Shen Ben*.(2013).A New Member of the 4-Methylideneimidazole-5-one-containing Aminomutase Family from the Enediyne Kedarcidin Biosynthetic Pathway.Proc. Natl. Acad. Sci. USA(110),8069-8074.
MLA	Huang Sheng-Xiong,et al."A New Member of the 4-Methylideneimidazole-5-one-containing Aminomutase Family from the Enediyne Kedarcidin Biosynthetic Pathway".Proc. Natl. Acad. Sci. USA .110(2013):8069-8074.