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Functional and structural characterization of IdnL7, an adenylation enzyme involved in incednine biosynthesis.


ABSTRACT: Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic, 5'-O-[N-(L-alanyl)sulfamoyl]adenosine, was determined at 2.1?Å resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small L-amino acids.

SUBMITTER: Cieslak J 

PROVIDER: S-EPMC6450520 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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Functional and structural characterization of IdnL7, an adenylation enzyme involved in incednine biosynthesis.

Cieślak Jolanta J   Miyanaga Akimasa A   Takaishi Makoto M   Kudo Fumitaka F   Eguchi Tadashi T  

Acta crystallographica. Section F, Structural biology communications 20190402 Pt 4


Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mim  ...[more]

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