The biochemical mechanisms of the plant activation of promutagenic aromatic amines

Journal Article · Mon Jan 01 04:00:00 EST 1990 · Environmental and Molecular Mutagenesis; (USA)

DOI:https://doi.org/10.1002/em.2850150411· OSTI ID:5623943

Wagner, E D; Verdier, M M; Plewa, M J ^[1]

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1. Univ. of Illinois, Urbana (USA)

Using specific monooxygenase and oxidase inhibitors in a plant cell/microbe coincubation assay, the biochemical mechanisms of the plant activation of two aromatic amines were compared. The biological endpoints included mutation induction, inhibition of mutagenicity, viability of the plant cells (activating system), and viability of the microbial cells. The activation of m-phenylenediamine by TX1 cells was mediated by enzyme systems that were inhibited by diethyldithiocarbamate, potassium cyanide, methimazole, (+)-catechin or acetaminophen. The inhibition by metyrapone was attended by toxicity in the plant cells. These data implicate a TX1 cell peroxidase and a FAD-dependent monoxygenase in the plant activation of m-phenylenediamine. The TX1 cell activation of 2-aminofluorene was inhibited by diethyldithiocarbamate, 7,8-benzoflavone, acetaminophen or (+)-catechin.

• OSTI ID: 5623943
• Journal Information: Environmental and Molecular Mutagenesis; (USA), Journal Name: Environmental and Molecular Mutagenesis; (USA) Vol. 15:4; ISSN 0893-6692; ISSN EMMUE
• Country of Publication: United States
• Language: English

Related Subjects

560300* -- Chemicals Metabolism & Toxicology
63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
AMINES
ARYL 4-MONOOXYGENASE
BIOCHEMISTRY
BIOLOGICAL EFFECTS
CARBAMATES
CARBONIC ACID DERIVATIVES
CARBOXYLIC ACID SALTS
CHEMISTRY
CYANIDES
ENZYME INHIBITORS
ENZYMES
METABOLIC ACTIVATION
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
OXIDOREDUCTASES
PLANT CELLS
POLYCYCLIC AROMATIC AMINES