Plant Phenylalanine/Tyrosine Ammonia-lyases

Barros, Jaime; Dixon, Richard A.

doi:10.1016/j.tplants.2019.09.011

Title: Plant Phenylalanine/Tyrosine Ammonia-lyases

Full Record
Other Related Research

Authors:: Barros, Jaime; Dixon, Richard A.

Publication Date:: Wed Jan 01 00:00:00 EST 2020

Sponsoring Org.:: USDOE

OSTI Identifier:: 1579777

Resource Type:: Publisher's Accepted Manuscript

Journal Name:: Trends in Plant Science

Additional Journal Information:: Journal Name: Trends in Plant Science Journal Volume: 25 Journal Issue: 1; Journal ID: ISSN 1360-1385

Publisher:: Elsevier

Country of Publication:: United Kingdom

Language:: English

Citation Formats


                    Barros, Jaime, and Dixon, Richard A. Plant Phenylalanine/Tyrosine Ammonia-lyases.  United Kingdom: N. p., 2020. 
Web.  doi:10.1016/j.tplants.2019.09.011.

Copy to clipboard


                    Barros, Jaime, & Dixon, Richard A. Plant Phenylalanine/Tyrosine Ammonia-lyases.  United Kingdom.  https://doi.org/10.1016/j.tplants.2019.09.011

Copy to clipboard


                    Barros, Jaime, and Dixon, Richard A. Wed .  
"Plant Phenylalanine/Tyrosine Ammonia-lyases".  United Kingdom.  https://doi.org/10.1016/j.tplants.2019.09.011.

Copy to clipboard


                    
@article{osti_1579777,

  title        = {Plant Phenylalanine/Tyrosine Ammonia-lyases},

  author       = {Barros, Jaime and Dixon, Richard A.},

  abstractNote = {},

  doi          = {10.1016/j.tplants.2019.09.011},

  journal      = {Trends in Plant Science},

  number       = 1,

  volume       = 25,

  place        = {United Kingdom},

  year         = {Wed Jan 01 00:00:00 EST 2020},

  month        = {Wed Jan 01 00:00:00 EST 2020}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Accepted Manuscript (Publisher)

Publisher's Version of Record
https://doi.org/10.1016/j.tplants.2019.09.011

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 81 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Structural Determinants And Modulation of Substrate Specificity in Phenylalanine-Tyrosine Ammonia-Lyases

Journal Article Louie, G V ; Bowman, M E ; Moffitt, M C ; ... - Chem.Biol.13:1327-1338,2006

No abstract prepared.
Induction of L-phenylalanine ammonia-lyase during utilization of phenylalanine as a carbon or nitrogen source in Rhodotorula glutinis

Journal Article Marusich, W C ; Jensen, R A ; Zamir, L O - J. Bacteriol.; (United States)

Rhodotorula glutinis is a convenient source of L-phenylalanine ammonia-lyase, an enzyme that is useful as a biochemical reagent in the assay of L-phenylalanine. There have been previous descriptions of induced lyase production in complex medium where induction occurs late in exponential growth, suggesting a role in secondary metabolism such as is the case in higher plants. A higher specific activity of L-phenylalanine ammonia-lyase (sixfold higher than in complex medium) can be obtained during midexponential growth in a defined medium containing L-phenylalanine as the sole source of carbon. L-phenylalanine will also induce lyase synthesis during exponential growth in minimal medium inmore »« less
Effects of CO/sub 2/ on total phenolics, phenylalanine ammonia lyase, and polyphenol oxidase in lettuce tissue

Journal Article Siriphanich, J ; Kader, A A - J. Am. Soc. Hortic. Sci.; (United States)

An atmosphere of air + 15% CO/sub 2/ caused CO/sub 2/ injury in lettuce (Lactuca sativa L.) in about 10 days at 0/sup 0/C. However, subsequent removal of CO/sub 2/ was necessary for the brown stain symptoms to develop. Under CO/sub 2/ treatment, phenylalanine ammonia lyase (PAL) was induced and its activity correlated well with the development of the injury. Nevertheless, PAL activity did not seem responsible for the differences in susceptibility to CO/sub 2/ injury among the 3 lettuce cultivars included in this study. Prevention of the development of brown stain symptoms by CO/sub 2/ probably was due tomore »« less
Phenylalanine ammonia lyase induced by ozone

Journal Article Kremer, D ; Howell, R K - Proc. Amer. Phytopathol. Soc.; (United States)

Ozone injured plant leaves typically show chlorosis, reddish-brown necrotic lesions, and premature senescence. Concentrations of caffeic acid derivatives are doubled and polymers of oxidized phenols and proteins accumulate in injured tissues. Precursors of plant phenols are synthesized by the enzyme phenylalanine ammonia lyase (PAL). The effect of zone on this enzyme was investigated. Thirty-day old Tempo bean plants were subjected to 8-10 pphm ozone for 5 hrs and the oldest trifoliate leaves analyzed for concentrations of PAL by determining cinnamic acid (CA) production spectrophotometrically at 290 nm. Mean concentrations of CA (nmoles CA/mg protein) of healthy tissues were 24.8, butmore »« less
RADIATION DAMAGE TO GRAPEFRUIT IN RELATION TO ETHYLENE PRODUCTION AND PHENYLALANINE AMMONIA-LYASE ACTIVITY.

Journal Article Riov, J ; Monselise, S P ; Kahan, R S - Radiat. Bot. 10: 281-6(Jun 1970).
https://doi.org/10.1016/S0033-7560(70)80022-9

Similar Records