Purification and characterization of an acyclic monoterpene primary alcohol:nadp+ oxidoreductase from catmint (Nepeta racemosa)

Hallahan, David L. and West, Jevon M. and Wallsgrove, Roger M. and Smiley, Diane W.M. and Dawson, Glenn W. and Pickett, John A. and Hamilton, James G.C. (1995) Purification and characterization of an acyclic monoterpene primary alcohol:nadp+ oxidoreductase from catmint (Nepeta racemosa). Archives of Biochemistry and Biophysics, 318 (1). pp. 105-112. ISSN 0003-9861

Full text not available from this repository.

Abstract

A soluble monoterpene primary alcohol:NADP+ oxidoreductase has been purified to apparent homogeneity from leaves of the catmint, Nepeta racemosa. The purified enzyme consisted of two polypeptides, with molecular masses of 42, 000 and 40, 000 Da, and contained zinc ions. A number of monoterpene alcohols (geraniol, nerol, citronellol, and their hydroxylated derivatives) were substrates, but the enzyme was inactive toward ethanol. The enzyme required NADP(H) as cofactor, with NAD(H) ineffective. Gas chromatographic and coupled mass spectrometric analysis of the reaction products showed that 10-hydroxygeraniol and 10-hydroxynerol were oxidized by the enzyme in the presence of NADP+, at both C-1 and C-10. These results are consistent with a role for this enzyme in the biosynthesis of iridoid monoterpenes.

Item Type:
Journal Article
Journal or Publication Title:
Archives of Biochemistry and Biophysics
Uncontrolled Keywords:
/dk/atira/pure/subjectarea/asjc/1300/1312
Subjects:
ID Code:
134459
Deposited By:
Deposited On:
22 Jun 2019 08:53
Refereed?:
Yes
Published?:
Published
Last Modified:
10 Jul 2020 06:28