In situ aldehyde generation for aldol addition reactions catalyzed by d-fructose-6-phosphate aldolase

Catalyst design in oxidation chemistry; from KMnO4 to artificial metalloenzymes

“…97 This system has the advantage that TEMPO is regenerated by the laccase, and therefore the methodology is not restricted by the substrate selectivity of the enzyme. 98 The laccase/TEMPO system has been shown to oxidize the primary hydroxyl group in monosaccharides and natural glycosides to acids under mild conditions (Scheme 15a and b). 99 A laccase/TEMPO system was applied for the formation of C-C bonds via an aldol addition, involving the in situ generation of the acceptor aldehyde (Scheme 15c).…”

Light‐Accelerated Biocatalytic Oxidation Reactions

“…Furthermore, the results presented herein may contribute to a better understanding of LMSs used in various applications. [29][30][31][38][39][40][41][42][43][44][45][46][47][48][49] Experimental Section…”

Chloroperoxidase-catalyzed amino alcohol oxidation: Substrate specificity and novel strategy for the synthesis of N -Cbz-3-aminopropanal

“…[24][25][26][27] In recent studies, some authors have chemically synthesized protected amino aldehydes. [28][29][30] Nevertheless, oxidative biocatalysis may have certain advantages over the chemical process: higher selectivity and hence more control and predictability of the obtained product structure, as well as fewer chemical reagents used. In a recent study, N-Cbz-3-aminopropanol oxidation was reported to be catalyzed by horse liver alcohol dehydrogenase; however, in this case, cofactor NADH regeneration was required.…”