Amino group modification functionalization

The preferred substrates of acetyltransferases are amino-groups of antibiotics, like chloramphenicol, strepto-gramin derivatives, and the various aminoglycosides. The modification is believed to block a functional group involved in the drug-target-interaction. All acetyltransferases use acetyl-coenzyme A as cofactor. 

Most immobilization methods require modification of the ligands for anchoring to the support by introducing functional groups such as vinyl, trialkoxysilyl, sulfonic acid, and amino groups. The consequence is often a more elaborate synthesis of the ligand, which adds to the costs of an immobilized catalyst. However, two interesting approaches were developed in recent years, when unmodi-... 

The above-described acylation of the sugar moiety of the nucleotide adenosine (3) [2] has been followed by a series of papers reporting on the chemoselec-tive enzymatic modification of natural compounds carrying both hydroxyl and amino groups. In addition to the extensive work on nucleosides developed by Gotor and coworkers [8], the biocatalyzed esterification of the hydroxylated alkaloids castanospermine (4) and 1-deoxynojirimidn (5) should be mentioned. Both compounds were selectively acylated at their C-6 and/or C-2 OH by the protease subtilisin, despite the presence of a potentially more reactive amino functions [9]. 

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