Hydroxylation of Limonene Enantiomers and Analogs by Recombinant (−)-Limonene 3- and 6-Hydroxylases from Mint (Mentha) Species: Evidence for Catalysis within Sterically Constrained Active Sites

Limonene enantiomers and substrate analogs, including specifically fluorinated derivatives, were utilized to probe active site interactions with recombinant (−)-(4S)-limonene-3-hydroxylase (CYP71D13) and (−)-(4S)-limonene-6-hydroxylase (CYP71D18) from mint (Mentha) species. (−)-(4S)-Limonene is hydr...

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Veröffentlicht in:Archives of biochemistry and biophysics 2001-03, Vol.387 (1), p.125-136
Hauptverfasser: Wüst, Matthias, Little, Dawn B, Schalk, Michel, Croteau, Rodney
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Sprache:eng
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