The biochemical mechanisms of the plant activation of promutagenic aromatic amines

Journal Article · Mon Jan 01 00:00:00 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), Vol. 15:4; ISSN 0893-6692
• Country of Publication: United States
• Language: English

Related Subjects

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