8j3o: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Formate dehydrogenase wild-type enzyme from Candida dubliniensis complexed with NADH== | |||
<StructureSection load='8j3o' size='340' side='right'caption='[[8j3o]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8j3o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_dubliniensis_CD36 Candida dubliniensis CD36]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8J3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8J3O 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]] 2.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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=8j3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j3o OCA], [https://pdbe.org/8j3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j3o RCSB], [https://www.ebi.ac.uk/pdbsum/8j3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j3o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B9WHT3_CANDC B9WHT3_CANDC] Catalyzes the NAD(+)-dependent oxidation of formate to carbon dioxide. Formate oxidation is the final step in the methanol oxidation pathway in methylotrophic microorganisms. Has a role in the detoxification of exogenous formate in non-methylotrophic organisms.[HAMAP-Rule:MF_03210] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nicotinamide adenine dinucleotide (NADH) and nicotinamide adenine dinucleotide phosphate (NADPH) constitute major hydrogen donors for oxidative/reductive bio-transformations. NAD(P)H regeneration systems coupled with formate dehydrogenases (FDHs) represent a dreamful method. However, most of the native FDHs are NAD(+) -dependent and suffer from insufficient reactivity compared to other enzymatic tools, such as glucose dehydrogenase. An efficient and competitive NADP(+) -utilizing FDH necessitates the availability and robustness of NADPH regeneration systems. Herein, we report the engineering of a new FDH from Candida dubliniensis (CdFDH), which showed no strict NAD(+) preference by a structure-guided rational/semi-rational design. A combinatorial mutant CdFDH-M4 (D197Q/Y198R/Q199N/A372S/K371T/triangle upQ375/K167R/H16L/K159R) exhibited 75-fold intensification of catalytic efficiency (k(cat) /K(m) ). Moreover, CdFDH-M4 has been successfully employed in diverse asymmetric oxidative/reductive processes with cofactor total turnover numbers (TTNs) ranging from 135 to 986, making it potentially useful for NADPH-required biocatalytic transformations. | |||
Engineering a Formate Dehydrogenase for NADPH Regeneration.,Ma W, Geng Q, Chen C, Zheng YC, Yu HL, Xu JH Chembiochem. 2023 Jul 16:e202300390. doi: 10.1002/cbic.202300390. PMID:37455264<ref>PMID:37455264</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8j3o" style="background-color:#fffaf0;"></div> | ||
[[Category: Geng | == References == | ||
[[Category: | <references/> | ||
[[Category: Zheng | __TOC__ | ||
</StructureSection> | |||
[[Category: Candida dubliniensis CD36]] | |||
[[Category: Large Structures]] | |||
[[Category: Chen C]] | |||
[[Category: Geng Q]] | |||
[[Category: Ma W]] | |||
[[Category: Zheng YC]] | |||
