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

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Purification and characterization of an acyclic monoterpene primary alcohol:nadp+ oxidoreductase from catmint (Nepeta racemosa). / Hallahan, David L.; West, Jevon M.; Wallsgrove, Roger M. et al.
In: Archives of Biochemistry and Biophysics, Vol. 318, No. 1, 10.05.1995, p. 105-112.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Hallahan, DL, West, JM, Wallsgrove, RM, Smiley, DWM, Dawson, GW, Pickett, JA & Hamilton, JGC 1995, 'Purification and characterization of an acyclic monoterpene primary alcohol:nadp+ oxidoreductase from catmint (Nepeta racemosa)', Archives of Biochemistry and Biophysics, vol. 318, no. 1, pp. 105-112. https://doi.org/10.1006/abbi.1995.1210

APA

Hallahan, D. L., West, J. M., Wallsgrove, R. M., Smiley, D. W. M., Dawson, G. W., Pickett, J. A., & Hamilton, J. 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), 105-112. https://doi.org/10.1006/abbi.1995.1210

Vancouver

Hallahan DL, West JM, Wallsgrove RM, Smiley DWM, Dawson GW, Pickett JA et al. Purification and characterization of an acyclic monoterpene primary alcohol:nadp+ oxidoreductase from catmint (Nepeta racemosa). Archives of Biochemistry and Biophysics. 1995 May 10;318(1):105-112. doi: 10.1006/abbi.1995.1210

Author

Hallahan, David L. ; West, Jevon M. ; Wallsgrove, Roger M. et al. / Purification and characterization of an acyclic monoterpene primary alcohol:nadp+ oxidoreductase from catmint (Nepeta racemosa). In: Archives of Biochemistry and Biophysics. 1995 ; Vol. 318, No. 1. pp. 105-112.

Bibtex

@article{0cb50e0c5390435c9e13dc80b6e0dbd4,
title = "Purification and characterization of an acyclic monoterpene primary alcohol:nadp+ oxidoreductase from catmint (Nepeta racemosa)",
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.",
keywords = "Biosynthesis, Catmint, Monoterpenes, Nepeta racemosa, Nepetalactone, Oxidoreductase, Purification",
author = "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.}",
year = "1995",
month = may,
day = "10",
doi = "10.1006/abbi.1995.1210",
language = "English",
volume = "318",
pages = "105--112",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "1",

}

RIS

TY - JOUR

T1 - Purification and characterization of an acyclic monoterpene primary alcohol:nadp+ oxidoreductase from catmint (Nepeta racemosa)

AU - Hallahan, David L.

AU - West, Jevon M.

AU - Wallsgrove, Roger M.

AU - Smiley, Diane W.M.

AU - Dawson, Glenn W.

AU - Pickett, John A.

AU - Hamilton, James G.C.

PY - 1995/5/10

Y1 - 1995/5/10

N2 - 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.

AB - 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.

KW - Biosynthesis

KW - Catmint

KW - Monoterpenes

KW - Nepeta racemosa

KW - Nepetalactone

KW - Oxidoreductase

KW - Purification

U2 - 10.1006/abbi.1995.1210

DO - 10.1006/abbi.1995.1210

M3 - Journal article

C2 - 7726550

AN - SCOPUS:0028926989

VL - 318

SP - 105

EP - 112

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 1

ER -