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(S)-limonene 7-monooxygenase

From Wikipedia, the free encyclopedia

In enzymology, a (S)-limonene 7-monooxygenase (EC 1.14.13.49) is an enzyme that catalyzes the chemical reaction

(−)-(S)-limonene + NADPH + H+ + O2 (−)-perillyl alcohol + NADP+ + H2O

The 4 substrates of this enzyme are (−)-(S)-limonene, NADPH, H+, and O2, whereas its 3 products are (−)-perillyl alcohol, NADP+, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is (S)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). Other names in common use include (−)-limonene 7-monooxygenase, (−)-limonene hydroxylase, (−)-limonene monooxygenase, and (−)-limonene,NADPH:oxygen oxidoreductase (7-hydroxylating). This enzyme participates in monoterpenoid biosynthesis and limonene and pinene degradation. It employs one cofactor, heme.

References

  • Karp F, Mihaliak CA, Harris JL, Croteau R (1990). "Monoterpene biosynthesis: specificity of the hydroxylations of (−)-limonene by enzyme preparations from peppermint (Mentha piperita), spearmint (Mentha spicata), and perilla (Perilla frutescens) leaves". Arch. Biochem. Biophys. 276 (1): 219–26. doi:10.1016/0003-9861(90)90029-X. PMID 2297225.


This page was last edited on 21 January 2024, at 22:15
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