View source for 8afv


==DaArgC3 - Engineered Formyl Phosphate Reductase with 3 substitutions (S178V, G182V, L233I)==
<StructureSection load='8afv' size='340' side='right'caption='[[8afv]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8afv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Denitrovibrio_acetiphilus_DSM_12809 Denitrovibrio acetiphilus DSM 12809]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AFV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=8afv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8afv OCA], [https://pdbe.org/8afv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8afv RCSB], [https://www.ebi.ac.uk/pdbsum/8afv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8afv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D4H3H4_DENA2 D4H3H4_DENA2] Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.[HAMAP-Rule:MF_00150]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Formate can be envisioned at the core of a carbon-neutral bioeconomy, where it is produced from CO(2) by (electro-)chemical means and converted into value-added products by enzymatic cascades or engineered microbes. A key step in expanding synthetic formate assimilation is its thermodynamically challenging reduction to formaldehyde. Here, we develop a two-enzyme route in which formate is activated to formyl phosphate and subsequently reduced to formaldehyde. Exploiting the promiscuity of acetate kinase and N-acetyl-gamma-glutamyl phosphate reductase, we demonstrate this phosphate (P(i))-based route in vitro and in vivo. We further engineer a formyl phosphate reductase variant with improved formyl phosphate conversion in vivo by suppressing cross-talk with native metabolism and interface the P(i) route with a recently developed formaldehyde assimilation pathway to enable C2 compound formation from formate as the sole carbon source in Escherichia coli. The P(i) route therefore offers a potent tool in expanding the landscape of synthetic formate assimilation.

Engineering a new-to-nature cascade for phosphate-dependent formate to formaldehyde conversion in vitro and in vivo.,Nattermann M, Wenk S, Pfister P, He H, Lee SH, Szymanski W, Guntermann N, Zhu F, Nickel L, Wallner C, Zarzycki J, Paczia N, Gaissert N, Francio G, Leitner W, Gonzalez R, Erb TJ Nat Commun. 2023 May 9;14(1):2682. doi: 10.1038/s41467-023-38072-w. PMID:37160875<ref>PMID:37160875</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8afv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Denitrovibrio acetiphilus DSM 12809]]
[[Category: Large Structures]]
[[Category: Erb TJ]]
[[Category: Nattermann M]]
[[Category: Pfister P]]
[[Category: Zarzycki J]]