Probing the regiospecificity of enzyme-catalyzed steroid glycosylation.
The potential of a uniquely permissive engineered glycosyltransferase (OleD ASP) as a catalyst for steroid glycosylation is highlighted. The ability of OleD ASP to glucosylate a range of cardenolides and bufadienolides was assessed using a rapid LC-UV/MS-SPE-NMR analytical platform. While a bias toward OleD-catalyzed C3 monoglucosylation was observed, subtle alterations of the steroidal architecture, in some cases, invoked diglucosylation or, in one case (digoxigenin), C12 glucosylation. This latter case represents the first, and highly efficient, synthesis of digoxigenin 12-O-β-D-glucoside.
Pharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin, Madison, Wisconsin 53705, USA.
Maoquan
M
Zhou
Yanpeng
Y
Hou
Adel
A
Hamza
Christophe
C
Pain
Chang-Guo
CG
Zhan
Tim S
TS
Bugni
Jon S
JS
Thorson
D002384:Catalysis; D004076:Digoxigenin / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D004354:Drug Screening Assays, Antitumor; D005960:Glucosides / Q000138:chemical synthesis* / Q000737:chemistry; D006031:Glycosylation; D016695:Glycosyltransferases / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D013237:Stereoisomerism; D013256:Steroids / Q000737:chemistry*
D005960:Glucosides; D013256:Steroids; C578105:digoxigenin 12-O-beta-D-glucoside; D016695:Glycosyltransferases; D004076:Digoxigenin