Immobilized lipase from Mucor miehei (RML) catalyzed the regioselective acylation of the C-2 side-chain of the C-alkyl resorcin[4]arene tetra-alcohol 1 in the 1,2-alternate form in organic solvents using vinyl acetate as acylating reagent. The influence of reaction parameters and solvent choice were also studied. Docking simulations allowed the determination of the binding geometry of 1, revealing the importance of Trp88 residue in stabilizing the Michaelis–Menten complex between enzyme and substrate.
Botta, B., Zappia, G., Tafi, A., Botta, M., Manetti, F., Cernia, E., et al. (2003). Erratum: Lipase-catalyzed regioselective acylation of resorcin[4]arenes. JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC, 21(4-6), 313-313 [10.1016/S1381-1177(02)00221-7].
Erratum: Lipase-catalyzed regioselective acylation of resorcin[4]arenes
TAFI, ANDREA;BOTTA, MAURIZIO;MANETTI, FABRIZIO;
2003-01-01
Abstract
Immobilized lipase from Mucor miehei (RML) catalyzed the regioselective acylation of the C-2 side-chain of the C-alkyl resorcin[4]arene tetra-alcohol 1 in the 1,2-alternate form in organic solvents using vinyl acetate as acylating reagent. The influence of reaction parameters and solvent choice were also studied. Docking simulations allowed the determination of the binding geometry of 1, revealing the importance of Trp88 residue in stabilizing the Michaelis–Menten complex between enzyme and substrate.
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https://hdl.handle.net/11365/30341
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