4f6l

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f6l OCA], [https://pdbe.org/4f6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f6l RCSB], [https://www.ebi.ac.uk/pdbsum/4f6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f6l ProSAT]</span></td></tr>

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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<ref>PMID:23070851</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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