Journal article
Induced phenylpropanoid metabolism during suberization and lignification: a comparative analysis
Journal of plant physiology, Vol.157(6), pp.601-607
2000
Handle:
https://hdl.handle.net/2376/103314
PMID: 11858251
Abstract
Induction of the biosynthesis of phenylpropanoids was monitored at the enzyme level through measurement of the temporal change in the activity of two marker enzymes of phenylpropanoid metabolism, phenylalanine ammonia-lyase, (PAL, E.C. 4.1.3.5) and 4-coumaryl-CoA ligase (4-CL, E.C. 6.2.1.12) and two marker enzymes for hydroxycinnamyl alcohol biosynthesis, cinnamoyl-CoA: NADP
+ oxidoreductase (CCR, E.C. 1.2.1.44) and cinnamyl alcohol dehydrogenase (CAD, E.C. 1.1.1.195) in both suberizing potato (
Solanum tuberosum) tubers and lignifying loblolly pine (
Pinus taeda) cell cultures. While measurable activities of PAL, 4-CL and CAD increased upon initiation of suberization in potato tubers, that of CCR did not. By contrast, all four enzymes were induced upon initiation of lignification in pine cell cultures. The lack of CCR induction in potato by wound treatment is consistent with the channelling of hydroxycinnamoyl-CoA derivatives away from monolignol formation and toward other hydroxycinnamoyl derivatives such as those that accumulate during suberization.
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Details
- Title
- Induced phenylpropanoid metabolism during suberization and lignification: a comparative analysis
- Creators
- Mark A Bernards - Department of Plant Sciences, University of Western Ontario, London ON, N6A 5B7 CanadaLyndia M Susag - Department of Chemistry, University of Calgary, Calgary AB, T2N 1N4 CanadaDiana L Bedgar - The Institute of Biological Chemistry, Washington State University, Pullman WA 99164-6340, USAAldwin M Anterola - The Institute of Biological Chemistry, Washington State University, Pullman WA 99164-6340, USANorman G Lewis - The Institute of Biological Chemistry, Washington State University, Pullman WA 99164-6340, USA
- Publication Details
- Journal of plant physiology, Vol.157(6), pp.601-607
- Academic Unit
- Biological Chemistry, Institute of
- Publisher
- Elsevier GmbH
- Identifiers
- 99900546534501842
- Language
- English
- Resource Type
- Journal article