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Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis

Nat Chem Biol. 2020-05; 
Alonzo DA, Chiche-Lapierre C, Tarry MJ, Wang J, Schmeing TM.
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PCR Cloning and Subcloning A gene construct for the A–KR–PCP module (NCBI: WP_007498213, residues 1–1,318) from B. stratosphericus LAMA 585 was synthesized as an Escherichia coli codonoptimized gene and cloned into a pET-11a vector by GenScript. Get A Quote

摘要

Nonribosomal depsipeptides are natural products composed of amino and hydroxy acid residues. The hydroxy acid residues often derive from α-keto acids, reduced by ketoreductase domains in the depsipeptide synthetases. Biochemistry and structures reveal the mechanism of discrimination for α-keto acids and a remarkable architecture: flanking intact adenylation and ketoreductase domains are sequences separated by >1,100 residues that form a split 'pseudoAsub' domain, structurally important for the depsipeptide module's synthetic cycle.

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