Abstract
Interrupted adenylation domains are enigmatic fusions, in which one enzyme is inserted into another to form a highly unusual bifunctional enzyme. We present the first crystal structure of an interrupted adenylation domain that reveals a unique embedded methyltransferase. The structure and functional data provide insight into how these enzymes N-methylate amino acid precursors en route to nonribosomal peptides.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adenosine Monophosphate / chemistry
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Amino Acids / chemistry*
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Catalysis
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Catalytic Domain
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Crystallography, X-Ray
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Enzymes / chemistry*
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Escherichia coli / metabolism
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Imines / chemistry
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Kinetics
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Methylation*
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Peptide Synthases / chemistry
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Peptides / chemistry*
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Protein Domains
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Substrate Specificity
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Time Factors
Substances
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Amino Acids
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Enzymes
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Imines
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Peptides
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Adenosine Monophosphate
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Peptide Synthases