Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Carrot cells detoxify N-phosphonoacetyl-L-aspartate by esterification.

S C Cole1, R J Yon

  • 1School of Biological Sciences and Environmental Health, Thames Polytechnic, London, U.K.

The Biochemical Journal
|November 1, 1988
PubMed
Summary

Carrot cells detoxify N-phosphonoacetyl-L-aspartate (PALA) by forming carboxylic esters, a unique tolerance mechanism not seen in other cells. This detoxification process involves specific enzymatic modifications of PALA.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Detoxification of N-(phosphonoacetyl)-L-aspartate by carrot cells in suspension culture.

Planta·2013
Same author

Wheat-germ aspartate transcarbamoylase: revised purification, stability and re-evaluation of regulatory kinetics in terms of the Monod-Wyman-Changeux model.

European journal of biochemistry·1999
Same author

Effects of lipids on nucleotide inhibition of wheat-germ aspartate transcarbamoylase: evidence of an additional level of control?

The Biochemical journal·1996
Same author

Amino-acid substitutions in the cleavage site of acyl-coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum: effect on proenzyme cleavage and activity.

Gene·1995
Same author

Endogenous polypeptide-chain length and partial sequence of aspartate transcarbamoylase from wheat, characterised by immunochemical and cDNA methods.

Biochimica et biophysica acta·1994
Same author

Acyl-coenzyme A: isopenicillin N acyltransferase from Penicillium chrysogenum: effect of amino acid substitutions at Ser227, Ser230 and Ser309 on proenzyme cleavage and activity.

FEMS microbiology letters·1994

Area of Science:

  • Biochemistry
  • Plant Physiology
  • Enzymology

Background:

  • Pyrimidine biosynthesis is crucial for cell growth.
  • N-phosphonoacetyl-L-aspartate (PALA) is a known inhibitor of pyrimidine biosynthesis.
  • Carrot cells exhibit unique tolerance to PALA compared to bacterial and mammalian cells.

Purpose of the Study:

  • To elucidate the detoxification mechanism of PALA in carrot cells.
  • To identify the chemical modifications involved in PALA tolerance.
  • To investigate the specificity of the detoxification process.

Main Methods:

  • Anion-exchange chromatography for isolating detoxified PALA.
  • Incubation with carboxylic-ester hydrolase to assess enzyme activity.
  • Gas-liquid chromatography (G.1.c.) analysis of hydrolysis products.

Related Experiment Videos

  • Comparative studies with succinate to determine specificity.
  • Main Results:

    • Carrot cells detoxify PALA by forming carboxylic esters, altering its charge.
    • Enzymatic hydrolysis of detoxified PALA with carboxylic-ester hydrolase restored its inhibitory activity.
    • G.1.c. analysis revealed the formation of mono- and di-carboxylic esters (methyl and ethyl).
    • The detoxification mechanism demonstrated high specificity for PALA, not affecting succinate.

    Conclusions:

    • Carrot cell PALA tolerance is mediated by esterification, a novel detoxification pathway.
    • The formation of carboxylic esters is the key step in PALA detoxification.
    • The observed specificity suggests a targeted enzymatic process for PALA metabolism in carrots.