Tertiary alcohol preferred: Hydroxylation of trans-3-methyl-L-proline with proline hydroxylases

• Christian Klein and
• Wolfgang Hüttel

Beilstein J. Org. Chem. 2011, 7, 1643–1647, doi:10.3762/bjoc.7.193

• Christian Klein Wolfgang Huttel Institute of Pharmaceutical Sciences, Department of Pharmaceutical and Medicinal Chemistry, Albert-Ludwigs-Universität Freiburg, Albertstr. 25, 79104 Freiburg, Germany 10.3762/bjoc.7.193 Abstract The enzymatic synthesis of tertiary alcohols by the stereospecific

Coupled chemo(enzymatic) reactions in continuous flow

• Ruslan Yuryev,
• Simon Strompen and
• Andreas Liese

Beilstein J. Org. Chem. 2011, 7, 1449–1467, doi:10.3762/bjoc.7.169

• conversions in the range of 95–98%. The continuous enzymatic synthesis of N-acetylneuraminic acid (17) from N-acetylglucosamine (GlcNAc, 14) in an enzyme membrane reactor employing two enzymes was developed by Kragl and coworkers [27]. In their coupled-reaction system the first enzyme GlcNAc 2-epimerase

• and Gröger [37], Strompen et al. developed a continuous chemo-enzymatic synthesis of ethyl (S)-3-(benzylamino)butanoate (48), which is a precursor to (S)-3-aminobutanoic acid. In contrast to the multistep enzymatic processes previously mentioned here, this transformation is carried out in a nonaqueous

• continuous multistep enzymatic synthesis of fine chemicals, where cofactor regeneration is required. In such cases the whole-cell in vivo approach is advantageous over in vitro approaches, because it is not necessary to use immobilization or nanofiltration membranes for the retention of small cofactor

A novel high-yield synthesis of aminoacyl p-nitroanilines and aminoacyl 7-amino-4-methylcoumarins: Important synthons for the synthesis of chromogenic/fluorogenic protease substrates

• Xinghua Wu,
• Yu Chen,
• Herve Aloysius and
• Longqin Hu

Beilstein J. Org. Chem. 2011, 7, 1030–1035, doi:10.3762/bjoc.7.117

• moderate to excellent yields (54–95%) of the desired Nα-protected aminoacyl-pNAs [16]. However, only Boc protected amino acids were used in the reported study, with three examples provided. The enzymatic synthesis of aminoacyl-pNAs was also reported recently [17]. Although this method is free of

Chemical aminoacylation of tRNAs with fluorinated amino acids for in vitro protein mutagenesis

• Shijie Ye,
• Allison Ann Berger,
• Dominique Petzold,
• Oliver Reimann,
• Benjamin Matt and
• Beate Koksch

Beilstein J. Org. Chem. 2010, 6, No. 40, doi:10.3762/bjoc.6.40

• are suitable for in vitro protein mutagenesis. Conclusion and Outlook The efficient chemical and enzymatic synthesis of three novel fluorinated aminoacyl-pdCpAs and Abu-pdCpA and their corresponding charged tRNAs is reported. These aminoacyl-tRNAs can be used for site-specific protein mutagenesis in a

Large- scale ruthenium- and enzyme- catalyzed dynamic kinetic resolution of (rac)-1-phenylethanol

• Krisztián Bogár,
• Belén Martín-Matute and
• Jan-E. Bäckvall

Beilstein J. Org. Chem. 2007, 3, No. 50, doi:10.1186/1860-5397-3-50

• chemistry.[27] In the course of the chemo-enzymatic synthesis of optically pure alcohols and esters, Candida antarctica lipase B (CALB) was found to be one of the most active and selective biocatalysts compared to other enzymes. Lipases do not need the presence of a cofactor and they can be employed in pure