8p5o
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8p5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p5o OCA], [https://pdbe.org/8p5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p5o RCSB], [https://www.ebi.ac.uk/pdbsum/8p5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p5o ProSAT]</span></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=8p5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p5o OCA], [https://pdbe.org/8p5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p5o RCSB], [https://www.ebi.ac.uk/pdbsum/8p5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p5o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/GRSB_ANEMI GRSB_ANEMI] This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Val, Orn and Leu. Activation sites for these AA consist of individual domains. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| - | Engineering of biosynthetic enzymes is increasingly employed to synthesize structural analogues of antibiotics. Of special interest are | + | Engineering of biosynthetic enzymes is increasingly employed to synthesize structural analogues of antibiotics. Of special interest are nonribosomal peptide synthetases (NRPSs) responsible for the production of important antimicrobial peptides. Here, directed evolution of an adenylation domain of a Pro-specific NRPS module completely switched substrate specificity to the non-standard amino acid piperazic acid (Piz) bearing a labile N-N bond. This success was achieved by UPLC-MS/MS-based screening of small, rationally designed mutant libraries and can presumably be replicated with a larger number of substrates and NRPS modules. The evolved NRPS produces a Piz-derived gramicidin S analogue. Thus, we give new impetus to the too-early dismissed idea that widely accessible low-throughput methods can switch the specificity of NRPSs in a biosynthetically useful fashion. |
| - | Directed Evolution of Piperazic Acid Incorporation by a Nonribosomal Peptide Synthetase.,Stephan P, Langley C, Winkler D, Basquin J, Caputi L, O'Connor SE, Kries H Angew Chem Int Ed Engl. 2023 | + | Directed Evolution of Piperazic Acid Incorporation by a Nonribosomal Peptide Synthetase.,Stephan P, Langley C, Winkler D, Basquin J, Caputi L, O'Connor SE, Kries H Angew Chem Int Ed Engl. 2023 Aug 28;62(35):e202304843. doi: , 10.1002/anie.202304843. Epub 2023 Jul 18. PMID:37326625<ref>PMID:37326625</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Proline activating adenylation domain of gramicidin S synthetase 2 - GrsB1-Acore
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