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Publication Abstract from PubMed

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.

Heterologous expression and structural characterisation of a pyrazinone natural product assembly line.,Wyatt MA, Mok MC, Junop M, Magarvey NA Chembiochem. 2012 Nov 5;13(16):2408-15. doi: 10.1002/cbic.201200340. Epub 2012, Oct 15. PMID:23070851^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.