Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Alcohol Oxidoreductases / chemistry
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Bacillus / enzymology
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Bacterial Proteins / chemistry
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Crystallography, X-Ray
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Depsipeptides / biosynthesis*
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Depsipeptides / chemistry
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Keto Acids / chemistry*
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Keto Acids / metabolism
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Lysine / metabolism
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Peptide Synthases / chemistry*
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Peptide Synthases / genetics
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Peptide Synthases / metabolism*
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Protein Conformation
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Protein Domains
Substances
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Bacterial Proteins
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Depsipeptides
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Keto Acids
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Alcohol Oxidoreductases
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polyketide synthase ketoreductase
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Peptide Synthases
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Lysine