Literature DB >> 8353850

Bioactivation of N-hydroxy-2-acetylaminofluorenes by N,O-acyltransferase: substituent effects on covalent binding to DNA.

L W Boteju1, P E Hanna.   

Abstract

N-Acetoxyarylamines are reactive metabolites that lead to arylamine adduct formation with biological macromolecules. A series of 7-substituted-N-hydroxy-2-acetylaminofluorenes were converted to reactive N-acetoxyarylamines by enzymatic N,O-acyltransfer in the presence of DNA. The N-arylhydroxamic acid substrates that contained electronegative 7-substituents formed greater amounts of DNA adducts than either the unsubstituted compound (N-OH-AAF) or those analogs that contained electron-donating groups in the 7-position. Glutathione did not decrease the rates of DNA adduct formation, but other nucleophiles, such as potassium O-ethylxanthate, thiourea and N-acetylmethionine, inhibited adduct formation by the 7-Br-substituted compound (7-Br-N-OH-AAF) and the unsubstituted parent compound (N-OH-AAF). Nucleophiles, reducing agents (e.g. ascorbic acid) and spin-trapping agents had minimal effect on DNA adduct formation by the bioactivated form of 7-acetyl-2-(N-hydroxy-acetylamino)fluorene (7-Ac-N-OH-AAF). Triethylphosphite, an agent that reacts with aryl nitrenes, caused a concentration-dependent reduction in the amount of DNA adduct formed subsequent to bioactivation of 7-Ac-N-OH-AAF, but did not influence adduct formation when N-OH-AAF and 7-Br-N-OH-AAF were the substrates. The results indicate that a change in the reaction mechanism(s) responsible for DNA adduct formation occurred when the strongly electronegative acetyl group was incorporated into the 7-position of N-OH-AAF. It is proposed that a nitrene intermediate is involved in the formation of covalent adducts with DNA when 7-Ac-N-OH-AAF is activated by N,O-acyltransfer.

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Year:  1993        PMID: 8353850     DOI: 10.1093/carcin/14.8.1651

Source DB:  PubMed          Journal:  Carcinogenesis        ISSN: 0143-3334            Impact factor:   4.944


  1 in total

1.  3-Hydroxylaminophenol mutase from Ralstonia eutropha JMP134 catalyzes a Bamberger rearrangement.

Authors:  A Schenzle; H Lenke; J C Spain; H J Knackmuss
Journal:  J Bacteriol       Date:  1999-03       Impact factor: 3.490

  1 in total

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