Deciphering the Biosynthetic Origin of l-allo-Isoleucine

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Abstract
The nonproteinogenic amino acid L-allo-isoleucine (L-allo-Ile) is featured in an assortment of life forms comprised of, but not limited to, bacteria, fungi, plants and mammalian systems including homo sapiens. Despite its ubiquity and function importance, the specific origins of this unique amino acid have eluded characterization. In this study, we describe the discovery and characterization of two enzyme pairs consisting of a pyridoxal 5’-phosphate (PLP)-linked aminotransferase and an unprecedented isomerase synergistically responsible for the biosynthesis of L-allo-Ile from L-isoleucine (L-Ile) in natural products. DsaD/DsaE from the desotamide biosynthetic pathway in Streptomyces scopuliridis SCSIO ZJ46, and MfnO/MfnH from the marformycin biosynthetic pathway in Streptomyces drozdowiczii SCSIO 10141 drive L-allo-Ile generation in each respective system. In vivo gene inactivations validated the importance of the DsaD/DsaE pair and MfnO/MfnH pair in L-allo-Ile unit biosynthesis. Inactivation of PLP-linke...
Funding Information
  • Ministry of Science and Technology of the People's Republic of China (2012AA092104)
  • National Natural Science Foundation of China (31400072, 41306146, 81425022)
  • Chinese Academy of Sciences (KGZD-EW-606, XDA11030403)
  • Special Financial Fund of Innovative Development of Marine Economic Demonstration Project (GD2012-D01-001)

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