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| | <StructureSection load='6pex' size='340' side='right'caption='[[6pex]], [[Resolution|resolution]] 1.58Å' scene=''> | | <StructureSection load='6pex' size='340' side='right'caption='[[6pex]], [[Resolution|resolution]] 1.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6pex]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Grape Grape]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PEX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6pex]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vitis_vinifera Vitis vinifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PEX FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VIT_09s0002g04300, VITISV_025327 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29760 Grape])</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]] 1.581Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pex OCA], [http://pdbe.org/6pex PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pex RCSB], [http://www.ebi.ac.uk/pdbsum/6pex PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pex 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=6pex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pex OCA], [https://pdbe.org/6pex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pex RCSB], [https://www.ebi.ac.uk/pdbsum/6pex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pex ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/2KGR_VITVI 2KGR_VITVI] Involved in the biosynthesis of L-tartarate from L-ascorbate (PubMed:31488549). Catalyzes the NAD(P)H-dependent reduction of 2-dehydro-L-idonate (2-keto-L-gulonate) to L-idonate (PubMed:31488549). Can also reduce hydroxypyruvate to glycerate, glyoxylate to glycolate and pyruvate to D-lactate (PubMed:31488549). Prefers NADPH to NADH as proton donor (PubMed:31488549).<ref>PMID:31488549</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6pex" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6pex" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Grape]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Crystal, S]] | + | [[Category: Vitis vinifera]] |
| - | [[Category: John, B B]] | + | [[Category: Crystal S]] |
| - | [[Category: Robert, D H]] | + | [[Category: John BB]] |
| - | [[Category: Yong, J]] | + | [[Category: Robert DH]] |
| - | [[Category: 2-keto-l-gulonic acid]] | + | [[Category: Yong J]] |
| - | [[Category: Ascorbic acid degradation]]
| + | |
| - | [[Category: D-isomer-specific 2-hydroxyacid dehydrogenase]]
| + | |
| - | [[Category: L-tartaric acid pathway]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
2KGR_VITVI Involved in the biosynthesis of L-tartarate from L-ascorbate (PubMed:31488549). Catalyzes the NAD(P)H-dependent reduction of 2-dehydro-L-idonate (2-keto-L-gulonate) to L-idonate (PubMed:31488549). Can also reduce hydroxypyruvate to glycerate, glyoxylate to glycolate and pyruvate to D-lactate (PubMed:31488549). Prefers NADPH to NADH as proton donor (PubMed:31488549).[1]
Publication Abstract from PubMed
Tartaric acid has high economic value as an antioxidant and flavorant in food and wine industries. l-Tartaric acid biosynthesis in wine grape (Vitis vinifera) uses ascorbic acid (vitamin C) as precursor, representing an unusual metabolic fate for ascorbic acid degradation. Reduction of the ascorbate breakdown product 2-keto-l-gulonic acid to l-idonic acid constitutes a critical step in this l-tartaric acid biosynthetic pathway. However, the underlying enzymatic mechanisms remain obscure. Here, we identified a V. vinifera aldo-keto reductase, Vv2KGR, with 2-keto-l-gulonic acid reductase activity. Vv2KGR belongs to the d-isomer-specific 2-hydroxyacid dehydrogenase superfamily and displayed the highest similarity to the hydroxyl pyruvate reductase isoform 2 in Arabidopsis thaliana Enzymatic analyses revealed that Vv2KGR efficiently reduces 2-keto-l-gulonic acid to l-idonic acid and uses NADPH as preferred coenzyme. Moreover, Vv2KGR exhibited broad substrate specificity toward glyoxylate, pyruvate, and hydroxypyruvate, having the highest catalytic efficiency for glyoxylate. We further determined the X-ray crystal structure of Vv2KGR at 1.58 A resolution. Comparison of the Vv2KGR structure with those of d-isomer-specific 2-hydroxyacid dehydrogenases from animals and microorganisms revealed several unique structural features of this plant hydroxyl pyruvate reductase. Substrate structural analysis indicated that Vv2KGR uses two modes (A and B) to bind different substrates. 2-Keto-l-gulonic acid displayed the lowest predicted free-energy binding to Vv2KGR among all docked substrates. Hence, we propose that Vv2KGR functions in l-tartaric acid biosynthesis. To the best of our knowledge, this is the first report of a d-isomer-specific 2-hydroxyacid dehydrogenase that reduces 2-keto-l-gulonic acid to l-idonic acid in plants.
An aldo-keto reductase with 2-keto-l-gulonate reductase activity functions in l-tartaric acid biosynthesis from vitamin C in Vitis vinifera.,Jia Y, Burbidge CA, Sweetman C, Schutz E, Soole K, Jenkins C, Hancock RD, Bruning JB, Ford CM J Biol Chem. 2019 Nov 1;294(44):15932-15946. doi: 10.1074/jbc.RA119.010196. Epub , 2019 Sep 4. PMID:31488549[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jia Y, Burbidge CA, Sweetman C, Schutz E, Soole K, Jenkins C, Hancock RD, Bruning JB, Ford CM. An aldo-keto reductase with 2-keto-l-gulonate reductase activity functions in l-tartaric acid biosynthesis from vitamin C in Vitis vinifera. J Biol Chem. 2019 Nov 1;294(44):15932-15946. doi: 10.1074/jbc.RA119.010196. Epub , 2019 Sep 4. PMID:31488549 doi:http://dx.doi.org/10.1074/jbc.RA119.010196
- ↑ Jia Y, Burbidge CA, Sweetman C, Schutz E, Soole K, Jenkins C, Hancock RD, Bruning JB, Ford CM. An aldo-keto reductase with 2-keto-l-gulonate reductase activity functions in l-tartaric acid biosynthesis from vitamin C in Vitis vinifera. J Biol Chem. 2019 Nov 1;294(44):15932-15946. doi: 10.1074/jbc.RA119.010196. Epub , 2019 Sep 4. PMID:31488549 doi:http://dx.doi.org/10.1074/jbc.RA119.010196
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