4tsk
From Proteopedia
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==Ketol-acid reductoisomerase from Alicyclobacillus acidocaldarius== | ==Ketol-acid reductoisomerase from Alicyclobacillus acidocaldarius== | ||
| - | <StructureSection load='4tsk' size='340' side='right' caption='[[4tsk]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4tsk' size='340' side='right'caption='[[4tsk]], [[Resolution|resolution]] 2.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4tsk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TSK OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4tsk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius_subsp._acidocaldarius_DSM_446 Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TSK FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tsk OCA], [https://pdbe.org/4tsk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tsk RCSB], [https://www.ebi.ac.uk/pdbsum/4tsk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tsk ProSAT]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ILVC_ALIAD ILVC_ALIAD] Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.[HAMAP-Rule:MF_00435]<ref>PMID:25849365</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | All members of the ketol-acid reductoisomerase (KARI) enzyme family characterized to date have been shown to prefer the nicotinamide adenine dinucleotide phosphate hydride (NADPH) cofactor to nicotinamide adenine dinucleotide hydride (NADH). However, KARIs with the reversed cofactor preference are desirable for industrial applications, including anaerobic fermentation to produce branched-chain amino acids. By applying insights gained from structural and engineering studies of this enzyme family to a comprehensive multiple sequence alignment of KARIs, we identified putative NADH-utilizing KARIs and characterized eight whose catalytic efficiencies using NADH were equal to or greater than NADPH. These are the first naturally NADH-preferring KARIs reported and demonstrate that this property has evolved independently multiple times, using strategies unlike those used previously in the laboratory to engineer a KARI cofactor switch. | ||
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| + | Uncovering rare NADH-preferring ketol-acid reductoisomerases.,Brinkmann-Chen S, Cahn JK, Arnold FH Metab Eng. 2014 Aug 27;26C:17-22. doi: 10.1016/j.ymben.2014.08.003. PMID:25172159<ref>PMID:25172159</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4tsk" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Ketol-acid reductoisomerase 3D structures|Ketol-acid reductoisomerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Alicyclobacillus acidocaldarius subsp. acidocaldarius DSM 446]] |
| - | + | [[Category: Large Structures]] | |
| - | [[Category: | + | [[Category: Arnold FH]] |
| - | [[Category: | + | [[Category: Brinkmann-Chen S]] |
| - | [[Category: | + | [[Category: Cahn JKB]] |
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| - | [[Category: | + | |
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Current revision
Ketol-acid reductoisomerase from Alicyclobacillus acidocaldarius
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