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   <subfield code="a">Plant enzymes participating in degradation of nitroaromatic compounds have not been biochemically characterized in details so far. From suspension culture of soapwort (Saponaria officinalis L.) we isolated a novel plant oxidoreductase involved in degradation of trinitrotoluene (TNT). The enzyme catalyses first steps of reduction of TNT nitro groups in the presence of NAD(P)H under anaerobic conditions. The enzyme is monomeric with molecular mass 29 kDa, its two isoforms have pI 4.8 and 5.1. According to the spectral and activation analysis the enzyme contains flavinmono-nucleotide as a prosthetic group. The structure properties suggest an evolutional relationship to oxophytodienoate reductase. The N-terminal amino acid sequence shows homology to family of Old Yellow Enzyme (E.C. 1.6.99.1).</subfield>
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