Journal
CHEMBIOCHEM
Volume 13, Issue 16, Pages 2408-2415Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.201200340
Keywords
biosynthesis; heterologous expression; nonribosomal assembly; precursor-directed biosynthesis; reductases
Funding
- NSERC [371576]
- Canadian Institute of Health Research Doctoral Research Award
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Through a number of strategies nonribosomal peptide assembly lines give rise to a metabolic diversity not possible by ribosomal synthesis. One distinction within nonribosomal assembly is that products are elaborated on an enzyme-tethered substrate, and their release is enzyme catalysed. Reductive release by NAD(P)H-dependent catalysts is one observed nonribosomal termination and release strategy. Here we probed the selectivity of a terminal reductase domain by using a full-length heterologously expressed nonribosomal peptide synthetase for the dipeptide aureusimine and were able to generate 17 new analogues. Further, we generated an X-ray structure of aureusimine terminal reductase to gain insight into the structural details associated with this enzymatic domain.
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