Journal:Acta Cryst F:S2053230X19002863
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| + | Adenylation enzymes are responsible for the selective incorporation of an appropriate carboxylate building block in the biosynthesis of nonribosomal peptides and related natural products. The substrate specificity of adenylation enzymes dictates the chemical structure of natural products. Understanding how adenylation enzymes recognize their own substrates is important for engineering biosynthetic pathways to produce novel compounds for drug discovery. | ||
| + | This paper describes the biochemical and structural analyses of adenylation enzyme IdnL7 involved in the biosynthesis of macrolactam antibiotic incednine. IdnL7 shows a broad substrate specificity for several small L-amino acids such as L-alanine and glycine. To obtain mechanistic insights into the substrate recognition of IdnL7, we determined the crystal structure of IdnL7 in complex with a reaction intermediate analog. IdnL7 has Cys217, Ala285 and Thr318 at the substrate binding pocket. These residues likely enable to accommodate various small L-amino acids as a substrate. This structural observation expands our understanding of the structure-function relationships of adenylation enzymes. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 13:59, 4 March 2019
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