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Inhibition of polyamine and spermine oxidases by polyamine analogues

The FEBS Journal, 2006
Polyamine oxidase (PAO) and spermine oxidase (SMO) are involved in the catabolism of polyamines – basic regulators of cell growth and proliferation. The discovery of selective inhibitors of PAO and SMO represents an important tool in studying the involvement of these enzymes in polyamine homeostasis and a starting point for the development of novel ...
Bianchi, M.   +6 more
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Characterization of maize polyamine oxidase

Phytochemistry, 1990
Some structural and biochemical characteristics of polyamine oxidase (PAO) purified from maize shoots have been examined. The enzyme has only alanine as N-terminal amino acid and its N-terminal sequence shows a significant degree of homology with tryptophan 2-monooxygenase from Pseudomonas syringae pv. savastanoi.
FEDERICO, RODOLFO   +4 more
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A radioisotopic assay for polyamine oxidase

Analytical Biochemistry, 1990
A new radioisotopic assay for polyamine oxidase with N1-acetylspermine as substrate is presented. A modified method for the chemical synthesis of radioactive N1-acetylspermine, which gave a good yield, is also described. The reaction mixture, containing N1-[14C]acetylspermine and tissue homogenate, was incubated for the enzyme reaction and applied to a
T, Kumazawa, H, Seno, O, Suzuki
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Inhibition of Polyamine Oxidases by Ifenprodil

Pharmacy and Pharmacology Communications, 1999
info:eu-repo/semantics ...
Badolo, Lassina   +3 more
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Polyamine Oxidases and Oxidized Polyamines

2021
Polyamine oxidases that act at the secondary amino group would be further subdivided according to whether diaminopropane or aminopropionaldehyde were among the products. The highest specific activity was found in the peroxisomal fraction, where its presence has been confirmed histochemically in both rat liver and kidney, although polyamine oxidase was ...
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Cytotoxicity of polyamines to Amoeba proteus: Role of polyamine oxidase

Cell Biology and Toxicology, 1996
It has been shown that oxidation of polyamines by polyamine oxidases can produce toxic compounds (H2O2, aldehydes, ammonia) and that the polyamine oxidase-polyamine system is implicated, in vitro, in the death of several parasites. Using Amoeba proteus as an in vitro model, we studied the cytotoxicity to these cells of spermine, spermidine, their ...
Schenkel, Eric   +3 more
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Inhibition and killing of fungi by the polyamine oxidase-polyamine system

Antonie van Leeuwenhoek, 1990
Both components of the polyamine oxidase (PAO)-polyamine system are known to be present in phagocytes and have thus been postulated to contribute to the antimicrobial activity of these cells. Therefore, the effects of the PAO-polyamine system on three medically important opportunistic fungi were examined.
S M, Levitz   +2 more
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Occurrence of polyamine oxidase in tissues of the catfish

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1987
1. Polyamine oxidase (PAO) activity was found in the brain, intestine, kidney and liver of the siluroid catfish using N1-acetylspermine as substrate. It was highest in the intestine and lowest in the brain. 2. Substrate specificity of the enzyme was tested in the intestine and liver and the highest activity was found with N1-acetylspermine, followed by
T, Kumazawa, O, Suzuki
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Polyamine oxidase in higher plants

Biochemical and Biophysical Research Communications, 1970
Abstract A polyamine-specific oxidase found in the leaves of barley and maize seedlings oxidises spermine optimally at pH 4.5, the products being hydrogen peroxide, 1-(3-aminopropyl) pyrroline and 1,3-diaminopropane. Spermidine and 3,3′-diaminodipropylamine were oxidised more slowly than spermine with an optimum at about pH 7.0.
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The Di- and Polyamine Oxidases of Plants

1988
Although 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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