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| | <StructureSection load='5x5u' size='340' side='right'caption='[[5x5u]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='5x5u' size='340' side='right'caption='[[5x5u]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5x5u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29145 Atcc 29145]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X5U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5X5U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5x5u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Azospirillum_brasilense Azospirillum brasilense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5X5U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x5t|5x5t]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">araE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192 ATCC 29145])</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=5x5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x5u OCA], [https://pdbe.org/5x5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5x5u RCSB], [https://www.ebi.ac.uk/pdbsum/5x5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5x5u ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5x5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x5u OCA], [http://pdbe.org/5x5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x5u RCSB], [http://www.ebi.ac.uk/pdbsum/5x5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x5u ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KGSDH_AZOBR KGSDH_AZOBR]] Catalyzes the NAD(P)(+)-dependent oxidation of alpha-ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Prefers NAD(+) to NADP(+) as a cosubstrate. Displays broad substrate specificity: exhibits the highest activity with alphaKGSA and succinic semialdehyde as substrates, but to a lesser extent, is also active with glutaraldehyde, benzaldehyde, and a number of aldehydes from C3 to C8.<ref>PMID:16835232</ref> | + | [https://www.uniprot.org/uniprot/KGSD1_AZOBR KGSD1_AZOBR] Catalyzes the NAD(P)(+)-dependent oxidation of alpha-ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Prefers NAD(+) to NADP(+) as a cosubstrate. Displays broad substrate specificity: exhibits the highest activity with alphaKGSA and succinic semialdehyde as substrates, but to a lesser extent, is also active with glutaraldehyde, benzaldehyde, and a number of aldehydes from C3 to C8.<ref>PMID:16835232</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 29145]] | + | [[Category: Azospirillum brasilense]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kim, K J]] | + | [[Category: Kim K-J]] |
| - | [[Category: Son, H F]] | + | [[Category: Son H-F]] |
| - | [[Category: Alpha-ketoglutarate semialdehyde dehydrogenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
KGSD1_AZOBR Catalyzes the NAD(P)(+)-dependent oxidation of alpha-ketoglutaric semialdehyde (alphaKGSA) to alpha-ketoglutarate. Is involved in a degradation pathway of L-arabinose that allows A.brasilense to grow on L-arabinose as a sole carbon source. Prefers NAD(+) to NADP(+) as a cosubstrate. Displays broad substrate specificity: exhibits the highest activity with alphaKGSA and succinic semialdehyde as substrates, but to a lesser extent, is also active with glutaraldehyde, benzaldehyde, and a number of aldehydes from C3 to C8.[1]
Publication Abstract from PubMed
3-Hydroxypropionic acid (3-HP) is an important platform chemical to be converted to acrylic acid and acrylamide. Aldehyde dehydrogenase (ALDH), an enzyme that catalyzes the reaction of 3-hydroxypropionaldehyde (3-HPA) to 3-HP, determines 3-HP production rate during the conversion of glycerol to 3-HP. To elucidate molecular mechanism of 3-HP production, we determined the first crystal structure of a 3-HP producing ALDH, alpha-ketoglutarate-semialdehyde dehydrogenase from Azospirillum basilensis (AbKGSADH), in its apo-form and in complex with NAD+. Although showing an overall structure similar to other ALDHs, the AbKGSADH enzyme had an optimal substrate binding site for accepting 3-HPA as a substrate. Molecular docking simulation of 3-HPA into the AbKGSADH structure revealed that the residues Asn159, Gln160 and Arg163 stabilize the aldehyde- and the hydroxyl-groups of 3-HPA through hydrogen bonds, and several hydrophobic residues, such as Phe156, Val286, Ile288, and Phe450, provide the optimal size and shape for 3-HPA binding. We also compared AbKGSADH with other reported 3-HP producing ALDHs for the crucial amino acid residues for enzyme catalysis and substrate binding, which provides structural implications on how these enzymes utilize 3-HPA as a substrate.
Structural insights into the production of 3-hydroxypropionic acid by aldehyde dehydrogenase from Azospirillum brasilense.,Son HF, Park S, Yoo TH, Jung GY, Kim KJ Sci Rep. 2017 Apr 10;7:46005. doi: 10.1038/srep46005. PMID:28393833[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Watanabe S, Kodaki T, Makino K. A novel alpha-ketoglutaric semialdehyde dehydrogenase: evolutionary insight into an alternative pathway of bacterial L-arabinose metabolism. J Biol Chem. 2006 Sep 29;281(39):28876-88. Epub 2006 Jul 11. PMID:16835232 doi:http://dx.doi.org/10.1074/jbc.M602585200
- ↑ Son HF, Park S, Yoo TH, Jung GY, Kim KJ. Structural insights into the production of 3-hydroxypropionic acid by aldehyde dehydrogenase from Azospirillum brasilense. Sci Rep. 2017 Apr 10;7:46005. doi: 10.1038/srep46005. PMID:28393833 doi:http://dx.doi.org/10.1038/srep46005
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