Chemo-enzymatic total synthesis: current approaches toward the integration of chemical and enzymatic transformations

• Ryo Tanifuji and
• Hiroki Oguri

Beilstein J. Org. Chem. 2024, 20, 1693–1712, doi:10.3762/bjoc.20.151

• Ryo Tanifuji Hiroki Oguri Department of Chemistry, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan 10.3762/bjoc.20.151 Abstract A steadily increasing number of reports have been published on chemo-enzymatic synthesis methods that integrate

• well as their analogs, is outlined with an emphasis on comparing these chemo-enzymatic syntheses with the corresponding natural biosynthetic pathways. Keywords: chemo-enzymatic synthesis; late-stage modification; reactive biosynthetic intermediate; regio- and stereoselective (macro)cyclization; total

• pathways are described with a focus on the biosynthetic intermediates and enzymatic transformations that enable cascade reactions and pinpoint modifications. This focus highlights how these biosynthetic pathways are applicable to the development of streamlined chemo-enzymatic synthesis processes. The

Chemo-enzymatic modification of poly-N-acetyllactosamine (LacNAc) oligomers and N,N-diacetyllactosamine (LacDiNAc) based on galactose oxidase treatment

• Christiane E. Kupper,
• Ruben R. Rosencrantz,
• Birgit Henßen,
• Helena Pelantová,
• Stephan Thönes,
• Anna Drozdová,
• Vladimir Křen and
• Lothar Elling

Beilstein J. Org. Chem. 2012, 8, 712–725, doi:10.3762/bjoc.8.80

• oligomers containing terminally and/or internally modified galactose residues were obtained, which can be used for binding studies and various other applications. Keywords: chemo-enzymatic synthesis; galactose oxidase; glycosyltransferase; LacDiNAc; poly-N-acetyllactosamine; Introduction N

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

• 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

• enzyme membrane reactors. E1: GDP-mannose pyrophosphorylase; E2: Pyrophosphatase [36]. Continuous solvent-free chemo-enzymatic synthesis of ethyl (S)-3-(benzylamino)butanoate (48) in a sequence of a plug-flow reactor (PFR) and a packed-bed reactor containing Novozym 435 (E) [38]. Continuous chemo

• -enzymatic synthesis of grossamide (52) in a cascade of packed-bed reactors. E: Peroxidase [39]. Chemo-enzymatic synthesis of 2-aminophenoxazin-3-one (56) in a cascade of continuously operating packed-bed microreactors. E1: Hydroxyaminobenzene mutase; E2: Soybean peroxidase [40]. Continuous conversion of 3

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