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. 1983 Apr;71(4):822–827. doi: 10.1104/pp.71.4.822

Changes in the Activities of Pyrrolooxygenases during the Germination of Wheat Grains 1

Adriana R Sburlati 1, Rosalía B Frydman 1
PMCID: PMC1066129  PMID: 16662914

Abstract

Porphobilinogen oxygenase, skatole pyrrolooxygenase, and tryptophan pyrrolooxygenase were found in the different parts of germinating wheat (Triticum aestivum) grain seedlings. In the embryos of grains germinated for 24 hours, the activities of PBG oxygenase and skatole pyrrolooxygenase were inhibited by a labile inhibitor. Tryptophan pyrrolooxygenase activity was not inhibited. Embryos of grains germinated for 48 hours showed higher activities for the three enzymes. The latter were also present in the radicles and coleoptiles of 96-hour germinated wheat grains. A DEAE-cellulose analysis of a crude enzymic preparation from embryos allowed the separation of two molecular forms of the three pyrrolooxygenases. The more cationic forms of porphobilinogen oxygenase and skatole pyrrolooxygenase were associated with the inhibitor. This form of porphobilinogen oxygenase had allosteric kinetics while the more anionic form had Michaelis kinetics. Both forms of skatole pyrrolooxygenase had Michaelis kinetics. The activity of tryptophan pyrrolooxygenase was highest in seedling roots and was found to be inhibited in seedling young leaves. This enzyme oxidized tryptophanyl dipeptides, as well as a nonapeptide, to N-formylkynurenine-containing peptides. The pyrrolooxygenase also oxidized the tryptophanyl residues of lysozyme, chymotrypsin, and trypsin.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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