2cf5
CRYSTAL STRUCTURES OF THE ARABIDOPSIS CINNAMYL ALCOHOL DEHYDROGENASES, ATCAD5
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OverviewOverview
The cinnamyl alcohol dehydrogenase (CAD) multigene family in planta, encodes proteins catalyzing the reductions of various phenylpropenyl, aldehyde derivatives in a substrate versatile manner, and whose metabolic, products are the precursors of structural lignins, health-related lignans, and various other metabolites. In Arabidopsis thaliana, the two isoforms, AtCAD5 and AtCAD4, are the catalytically most active being viewed as, mainly involved in the formation of guaiacyl/syringyl lignins. In this, study, we determined the crystal structures of AtCAD5 in the apo-form and, as a binary complex with NADP+, respectively, and modeled that of AtCAD4., Both AtCAD5 and AtCAD4 are dimers with two zinc ions per subunit and, belong to the Zn-dependent medium chain dehydrogenase/reductase (MDR), ... [(full description)]
About this StructureAbout this Structure
2CF5 is a [Single protein] structure of sequence from [Arabidopsis thaliana] with ZN as [ligand]. Active as [Cinnamyl-alcohol dehydrogenase], with EC number [1.1.1.195]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4., Youn B, Camacho R, Moinuddin SG, Lee C, Davin LB, Lewis NG, Kang C, Org Biomol Chem. 2006 May 7;4(9):1687-97. Epub 2006 Apr 4. PMID:16633561
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