5vkt
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cinnamyl alcohol dehydrogenases (SbCAD4) from Sorghum bicolor (L.) Moench== | |
| + | <StructureSection load='5vkt' size='340' side='right' caption='[[5vkt]], [[Resolution|resolution]] 1.83Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5vkt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VKT FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLT:D-MALATE'>MLT</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cinnamyl-alcohol_dehydrogenase Cinnamyl-alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.195 1.1.1.195] </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=5vkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vkt OCA], [http://pdbe.org/5vkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vkt RCSB], [http://www.ebi.ac.uk/pdbsum/5vkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vkt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cinnamyl alcohol dehydrogenase (CAD) catalyzes the final step in monolignol biosynthesis, reducing sinapaldehyde, coniferaldehyde, and p-coumaraldehyde to their corresponding alcohols in an NADPH-dependent manner. Because of its terminal location in monolignol biosynthesis, the variation in substrate specificity and activity of CAD can result in significant changes in overall composition and amount of lignin. Our in-depth characterization of two major CAD isoforms, SbCAD2 (Brown midrib 6 [bmr6]) and SbCAD4, in lignifying tissues of sorghum (Sorghum bicolor), a strategic plant for generating renewable chemicals and fuels, indicates their similarity in both structure and activity to Arabidopsis (Arabidopsis thaliana) CAD5 and Populus tremuloides sinapyl alcohol dehydrogenase, respectively. This first crystal structure of a monocot CAD combined with enzyme kinetic data and a catalytic model supported by site-directed mutagenesis allows full comparison with dicot CADs and elucidates the potential signature sequence for their substrate specificity and activity. The L119W/G301F-SbCAD4 double mutant displayed its substrate preference in the order coniferaldehyde > p-coumaraldehyde > sinapaldehyde, with higher catalytic efficiency than that of both wild-type SbCAD4 and SbCAD2. As SbCAD4 is the only major CAD isoform in bmr6 mutants, replacing SbCAD4 with L119W/G301F-SbCAD4 in bmr6 plants could produce a phenotype that is more amenable to biomass processing. | ||
| - | + | The Enzyme Activity and Substrate Specificity of Two Major Cinnamyl Alcohol Dehydrogenases in Sorghum (Sorghum bicolor), SbCAD2 and SbCAD4.,Jun SY, Walker AM, Kim H, Ralph J, Vermerris W, Sattler SE, Kang C Plant Physiol. 2017 Aug;174(4):2128-2145. doi: 10.1104/pp.17.00576. Epub 2017 Jun, 12. PMID:28606901<ref>PMID:28606901</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5vkt" style="background-color:#fffaf0;"></div> |
| - | [[Category: Jun, S | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cinnamyl-alcohol dehydrogenase]] | ||
| + | [[Category: Jun, S Y]] | ||
[[Category: Kang, C]] | [[Category: Kang, C]] | ||
| + | [[Category: Walker, A M]] | ||
| + | [[Category: Cad]] | ||
| + | [[Category: Cinnamyl alcohol dehydrogenase]] | ||
| + | [[Category: Coniferaldehyde]] | ||
| + | [[Category: Dehydrogenase]] | ||
| + | [[Category: Nadp+]] | ||
| + | [[Category: Nadph]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: P-coumaraldehyde]] | ||
| + | [[Category: Sad]] | ||
| + | [[Category: Sinapaldehyde]] | ||
| + | [[Category: Sinapyl alchohl dehydrogenase]] | ||
| + | [[Category: Sorghum]] | ||
Revision as of 09:01, 9 August 2017
Cinnamyl alcohol dehydrogenases (SbCAD4) from Sorghum bicolor (L.) Moench
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