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. 1967 Sep;104(3):1048–1055. doi: 10.1042/bj1041048

The inactivation of pea-seedling diamine oxidase by peroxidase and 1,5-diaminopentane

J M Hill 1
PMCID: PMC1271250  PMID: 4963523

Abstract

1. The rate of oxidative deamination of 1,5-diaminopentane by pea-seedling extracts, which contain diamine oxidase [diamine–oxygen oxidoreductase (deaminating), EC 1.4.3.6], was increased by adding pyridoxal or pyridoxal phosphate. 2. Evidence was obtained that pyridoxal does not activate the apoenzyme of diamine oxidase, but prevents the inactivation of the enzyme. 3. This inactivation only occurred when 1,5-diaminopentane was the substrate and depended on a second thermolabile factor in the extract besides the diamine oxidase. 4. Purified diamine oxidase, when catalysing the oxidation of 1,5-diaminopentane, was rapidly inactivated in the presence of peroxidase. 5. The inactivation was prevented not only by pyridoxal and pyridoxal phosphate but also by several unrelated compounds including α-oxoglutarate, catechol and o-aminobenzaldehyde. 6. It is suggested that peroxidase catalyses the further oxidation of the product of the oxidative deamination of 1,5-diaminopentane to a compound that inactivates diamine oxidase. 7. The results diminish the relevance of previous evidence that plant diamine oxidase contains pyridoxal phosphate.

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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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