Acid-catalyzed enzymatic hydrolysis of 1-methylcyclohexene oxide

Citation
Mj. Van Der Werf et al., Acid-catalyzed enzymatic hydrolysis of 1-methylcyclohexene oxide, TETRAHEDR-A, 10(21), 1999, pp. 4225-4230
Citations number
19
Categorie Soggetti
Organic Chemistry/Polymer Science
Journal title
TETRAHEDRON-ASYMMETRY
ISSN journal
09574166 → ACNP
Volume
10
Issue
21
Year of publication
1999
Pages
4225 - 4230
Database
ISI
SICI code
0957-4166(19991029)10:21<4225:AEHO1O>2.0.ZU;2-2
Abstract
Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14, an enzy me involved in the limonene metabolism of this microorganism, catalyzes the enantioselective hydrolysis of 1-methylcyclohexene oxide. (1R,2S)-1-Methyl cyclohexene oxide was the preferred substrate and it was mainly hydrolyzed to (1S,2S)-1 methylcyclohexane-1,2-diol, while (1S,2R)-1-methylcyclohexene oxide was converted more slowly and mainly yielded (1R,2R)-1-methylcyclohex ane-1,2-diol. The reaction proceeded with a high regioselectivity (C1:C2, 8 5,15). (H2O)-O-18-labelling experiments confirmed that the nucleophile was mainly incorporated at the most substituted carbon atom, suggesting that li monene-1,2-epoxide hydrolase uses an acid-catalyzed enzyme mechanism. (C) 1 999 Elsevier Science Ltd. All rights reserved.