Enzymatic removal of carboxyl protecting groups. 1. Cleavage of the tert-butyl moiety.
[reaction: see text] A recent discovery that a certain amino acid motif (GGG(A)X-motif) in lipases and esterases determines their activity toward tertiary alcohols prompted us to investigate the use of these biocatalysts in the mild and selective removal of tert-butyl protecting groups in amino acid derivatives and related compounds. An esterase from Bacillus subtilis (BsubpNBE) and lipase A from Candida antarctica (CAL-A) were identified as the most active enzymes, which hydrolyzed a range of tert-butyl esters of protected amino acids (e.g., Boc-Tyr-O(t)Bu, Z-GABA-O(t)Bu, Fmoc-GABA-O(t)Bu) in good to high yields and left Boc, Z, and Fmoc-protecting groups intact.
Schmidt
Marlen
M
Department of Technical Chemistry and Biotechnology, Institute of Chemistry and Biochemistry, Greifswald University, Soldmannstr. 16, D-17487 Greifswald, Germany.
Barbayianni
Efrosini
E
Fotakopoulou
Irene
I
Höhne
Matthias
M
Constantinou-Kokotou
Violetta
V
Bornscheuer
Uwe T
UT
Kokotos
George
G
D000595:Amino Acid Sequence; D000596:Amino Acids; D001412:Bacillus subtilis / Q000201:enzymology*; D001555:Benzene Derivatives / Q000378:metabolism*; D002073:Butanes / Q000138:chemical synthesis / Q000378:metabolism; D002176:Candida albicans / Q000201:enzymology*; D002264:Carboxylic Acids / Q000378:metabolism; D002384:Catalysis; D004950:Esterases / Q000378:metabolism*; D006846:Hydrocarbons, Halogenated / Q000378:metabolism*; D007202:Indicators and Reagents; D008049:Lipase / Q000378:metabolism*
D000596:Amino Acids; D001555:Benzene Derivatives; D002073:Butanes; D002264:Carboxylic Acids; D006846:Hydrocarbons, Halogenated; D007202:Indicators and Reagents; D004950:Esterases; D008049:Lipase