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| | ==4-hydroxyisoleucine dehydrogenase mutant complexed with NADH and succinate== | | ==4-hydroxyisoleucine dehydrogenase mutant complexed with NADH and succinate== |
| - | <StructureSection load='5gwt' size='340' side='right' caption='[[5gwt]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='5gwt' size='340' side='right'caption='[[5gwt]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gwt]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._thuringiensis"_smith_et_al._1952 "bacillus cereus var. thuringiensis" smith et al. 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GWT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gwt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GWT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gwr|5gwr]], [[5gws|5gws]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AC241_05390 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1428 "Bacillus cereus var. thuringiensis" Smith et al. 1952])</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=5gwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gwt OCA], [https://pdbe.org/5gwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gwt RCSB], [https://www.ebi.ac.uk/pdbsum/5gwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gwt ProSAT]</span></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=5gwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gwt OCA], [http://pdbe.org/5gwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gwt RCSB], [http://www.ebi.ac.uk/pdbsum/5gwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gwt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0K0Q8K4_BACTU A0A0K0Q8K4_BACTU] |
| | <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: Bacillus cereus var. thuringiensis smith et al. 1952]] | + | [[Category: Bacillus thuringiensis]] |
| - | [[Category: Miyakawa, T]] | + | [[Category: Large Structures]] |
| - | [[Category: Nakamura, A]] | + | [[Category: Miyakawa T]] |
| - | [[Category: Shi, X]] | + | [[Category: Nakamura A]] |
| - | [[Category: Tanokura, M]] | + | [[Category: Shi X]] |
| - | [[Category: Dehydrogenase]]
| + | [[Category: Tanokura M]] |
| - | [[Category: Nadh-dependent]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Reductase]]
| + | |
| - | [[Category: Short-chain]]
| + | |
| Structural highlights
Function
A0A0K0Q8K4_BACTU
Publication Abstract from PubMed
Fenugreek is a dietary supplement for anti-aging and human health. (2S,3R,4S)-4-hydroxyisoleucine (4-HIL), which is extracted from fenugreek seeds, is expected to be a promising orally active drug for diabetes and diabetic nephropathy because of its insulinotropic effect. Although several chemical synthesis methods of 4-HIL have been proposed, these methods require multistep reactions to control the stereochemistry of 4-HIL. In this study, we modified the key enzyme 4-HIL dehydrogenase (HILDH) to overcome the biggest limitation in commercial-scale production of 4-HIL. As a result, an effective one-step carbonyl reduction to produce (2S,3R,4S)-4-HIL was successfully accomplished with strict stereoselectivity (>99% de). Mass production of (2S,3R,4S)-4-HIL by our synthetic method could have a significant contribution to the prevention of diabetes, dyslipidemia, and Alzheimer's disease. (120 words/200 words).
Engineering a short-chain dehydrogenase/reductase for the stereoselective production of (2S,3R,4S)-4-hydroxyisoleucine with three asymmetric centers.,Shi X, Miyakawa T, Nakamura A, Hou F, Hibi M, Ogawa J, Kwon Y, Tanokura M Sci Rep. 2017 Oct 20;7(1):13703. doi: 10.1038/s41598-017-13978-w. PMID:29057974[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shi X, Miyakawa T, Nakamura A, Hou F, Hibi M, Ogawa J, Kwon Y, Tanokura M. Engineering a short-chain dehydrogenase/reductase for the stereoselective production of (2S,3R,4S)-4-hydroxyisoleucine with three asymmetric centers. Sci Rep. 2017 Oct 20;7(1):13703. doi: 10.1038/s41598-017-13978-w. PMID:29057974 doi:http://dx.doi.org/10.1038/s41598-017-13978-w
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