4906-24-5Relevant articles and documents
A multicatalyst system for the one-pot desymmetrization/oxidation of meso-1,2-alkane diols
Mueller, Christian E.,Hrdina, Radim,Wende, Raffael C.,Schreiner, Peter R.
supporting information; experimental part, p. 6309 - 6314 (2011/08/07)
Two is better than one: We demonstrate the viability of an organocatalytic reaction sequence along a short peptide backbone that carries two independent catalytic functionalities, which allow the rapid, one-pot acylative desymmetrization and oxidation of meso-alkane-1,2-diols to the corresponding acetylated acetoins with good yields and enantioselectivities (see scheme). Copyright
One-Pot desymmetrization of meso-l,2-hydrocarbon diols through acylation and oxidation
Mueller, Christian E.,Zell, Daniela,Schreiner, Peter R.
supporting information; experimental part, p. 9647 - 9650 (2010/04/28)
Avoid racemization! Short lipophilic oligopeptides utilizing nucleophilic N-jt-methyl histidine residues catalyze the desymmetrization of wieso-l,2-diols with enantiomeric ratios of up to 94:6. Direct one-pot oxidation, which avoids the well-known racemiz
Asymmetric Reduction of 1-Acetoxy-2-alkanones with Baker's Yeast: Purification and Characterization of α-Acetoxy Ketone Reductase
Ishihara, Kohji,Nakajima, Nobuyoshi,Tsuboi, Sadao,Utaka, Masanori
, p. 3314 - 3319 (2007/10/02)
An α-acetoxy ketone reducing enzyme has been purified and characterized from the cell-free extract of bakers' yeast (Saccharomyces cerevisiae). Only one NADPH-dependent dehydrogenase that catalyzed the reduction of α-acetoxy ketone was found in bakers' yeast. The molecular weight of the enzyme was estimated to be 36 kDa by SDS-polyacrylamide gel electrophoresis. The enzyme was composed of a single polypeptide chain. The enzyme had reducing activity for both aliphatic and aromatic α-acetoxy ketones, although no reducing activity toward α-chloro ketones and α-hydroxy ketones was found. The enzyme catalyzed the reduction of not only α-acetoxy ketones, but also β-keto esters. Studies on the chromatographic behavior and stereospecificity indicated that the enzyme was identical with one of the β-keto ester reductases purified from bakers' yeast.