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The Di- and Polyamine Oxidases of Plants
1988Although the di- and polyamine oxidases of plants are apparently limited in their distribution, in some species they are remarkably active. Earlier work on these enzymes has been summarized by Smith (1985a), Morgan (1985), Rinaldi et al., (1986), and Mondovi and Avigliano (1987).
T A, Smith, J H, Barker
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Polyamine oxidase from Zea mays shoots
Phytochemistry, 1973Abstract Polyamine oxidase of maize shoots purified 10-fold had a pH optimum of 6·3 with spermidine as substrate, and Km of 6 × 10−4 M. The enzyme was inhibited by the acridine compounds quinacrine, 6,9-diamino-2-ethoxyacridine and acriflavin, but carbonyl reagents, typical thiol inhibitors and copper-binding agents were without effect. Inhibition by
Yonezo Suzuki, Eiji Hirasawa
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Jasmonate‐mediated polyamine oxidase 6 drives herbivore‐induced polyamine catabolism in rice
The Plant JournalSUMMARYPolyamines (PAs) along with their conjugated forms, are important mediators of plant defense mechanisms against both biotic and abiotic stresses. Flavin‐containing polyamine oxidases (PAOs) regulate PA levels through terminal oxidation. To date, the role of PAOs in plant–herbivore interaction remains poorly understood.
Hongyue Zu +7 more
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Polyamine oxidase from barley and oats
Phytochemistry, 1976Abstract The pH optimum for the stability of the barley leaf polyamine oxidase is 4.8, which is also the pH optimum for its activity with spermine as substrate. Zonal centrifugation indicates that the enzyme is associated with a particle which is slightly more dense than chloroplasts, and the peak of activity corresponds with the peak of nucleic acid.
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Polyamine oxidase, properties and functions.
Progress in brain research, 1996Polyamine oxidase (PAO) is a FAD-dependent enzyme with a molecular mass of about 62 kDa, present with high activity in most tissues of vertebrates. Structural requirements of a substrate for PAO are two positively charged amino groups, separated by a short carbon chain and an alkyl substituent on one or both nitrogen atoms.
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Polyamine oxidases — enzymes of unknown function?
Biochemical Society Transactions, 1998openaire +2 more sources
Inhibition of human neutrophil locomotion by the polyamine oxidase-polyamine system.
Immunology, 1985The polyamines, spermine and spermidine, in the presence of either bovine serum [containing polyamine oxidase (PAO) activity] or partially purified PAO, inhibited human neutrophil locomotion. This effect could not be produced by either bovine serum, PAO, or the polyamines alone.
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