We modified a peptide that forms a homotrimeric coiled-coil with DNA handles, leading to a three-way peptide−DNA junction. This hybrid assembly could organize DNA tiles into trimeric species, or close up a triangular DNA base into a hybrid peptid...
Extended scope and understanding of zinc‐dependent alcohol dehydrogenases for reduction of cyclic α‐diketones
Von Wiley-VCH zur Verfügung gestellt
Alcohol dehydrogenases (ADH) are important tools for generating chiral a-hydroxyketones. Previously, only the ADH of Thauera aromatica was known to convert cyclic a-diketones with appropriate preference. Here, we extend the spectrum of suitable enzymes by three alcohol dehydrogenases from Citrifermentans bemidjiense (CibADH), Deferrisoma camini (DecADH), and Thauera phenylacetica (ThpADH). Of these, DecADH is characterized by very high thermostability; CibADH and ThpADH convert a-halogenated cyclohexanones with increased activity. Otherwise, however, the substrate spectrum of all four ADHs is highly conserved. Structural considerations led to the conclusion that conversion of diketones requires not only the expansion of the active site into a large binding pocket, but also the circumferential modification of almost all amino acid residues that form the first shell of the binding pocket. The constellation appears to be overall highly specific for the relative positioning of the carbonyl functions and the size of the C-ring.Zum Volltext
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