Carbohydrate PEGylation, an approach to improve pharmacological potency

• M. Eugenia Giorgi,
• Rosalía Agusti and
• Rosa M. de Lederkremer

Beilstein J. Org. Chem. 2014, 10, 1433–1444, doi:10.3762/bjoc.10.147

• PEGylation of a glycoprotein can be performed in three steps. First, the sialic acid is removed from the native protein with a sialidase and subsequently Sia-PEG is transfered to the uncovered terminal Gal units of the linked glycan taking advantage of the substrate promiscuity of the sialyltransferase

Quantification of N-acetylcysteamine activated methylmalonate incorporation into polyketide biosynthesis

• Stephan Klopries,
• Uschi Sundermann and
• Frank Schulz

Beilstein J. Org. Chem. 2013, 9, 664–674, doi:10.3762/bjoc.9.75

• promiscuity of wild type MatB malonyl-CoA synthetases was recently described [40], pointing out the need for an artificial and versatile activation mechanism as described here, to enable what we have termed enzyme-directed mutasynthesis. Conclusion Based on the single incorporation of 4 a relative

Natural product biosyntheses in cyanobacteria: A treasure trove of unique enzymes

• Jan-Christoph Kehr,
• Douglas Gatte Picchi and
• Elke Dittmann

Beilstein J. Org. Chem. 2011, 7, 1622–1635, doi:10.3762/bjoc.7.191

• marine cyanobacterium [69]. A single LanM-type enzyme, ProcM, was found to cooperate with 29 different precursor peptides in vitro and in vivo. The enzyme thus showed a remarkable catalytic promiscuity. The precursor peptides were encoded either cis or trans to the ProcM enzyme, and the resulting family