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EC 1.5.3.17 Details

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EC number

1.5.3.17

Accepted name

non-specific polyamine oxidase

Reaction

(1) spermine + O₂ + H₂O = spermidine + 3-aminopropanal + H₂O₂;;(2) spermidine + O₂ + H₂O = putrescine + 3-aminopropanal + H₂O₂;;(3) N¹-acetylspermine + O₂ + H₂O = spermidine + 3-acetamidopropanal + H₂O₂;;(4) N¹-acetylspermidine + O₂ + H₂O = putrescine + 3-acetamidopropanal + H₂O₂

Other name(s)

polyamine oxidase (ambiguous), Fms1, AtPAO3

Systematic name

polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming)

Comment

A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N⁸-acetylspermidine [3]. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine [2]. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines [1]. The specific polyamine oxidases are classified as EC 1.5.3.13 (N¹-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N⁸-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 1.5.3.16 (spermine oxidase).

History

created 2009

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.2 With a cytochrome as acceptor

1.1.3 With oxygen as acceptor

1.1.4 With a disulfide as acceptor

1.1.5 With a quinone or similar compound as acceptor

1.1.5.1 created 1983, deleted 2002

1.1.5.2 glucose 1-dehydrogenase (PQQ, quinone)

1.1.5.3 glycerol-3-phosphate dehydrogenase

1.1.5.4 malate dehydrogenase (quinone)

1.1.5.5 alcohol dehydrogenase (quinone)

1.1.5.6 formate dehydrogenase-N

1.1.5.7 cyclic alcohol dehydrogenase (quinone)

1.1.5.8 quinate/shikimate dehydrogenase (quinone)

1.1.5.9 glucose 1-dehydrogenase (FAD, quinone)

1.1.5.10 D-2-hydroxyacid dehydrogenase (quinone)

1.1.5.11 1-butanol dehydrogenase (quinone)

1.1.5.12 D-lactate dehydrogenase (quinone)

1.1.5.13 (S)-2-hydroxyglutarate dehydrogenase

1.1.5.14 fructose 5-dehydrogenase

1.1.7 With an iron-sulfur protein as acceptor

1.1.9 With a copper protein as acceptor

1.1.98 With other, known, physiological acceptors

1.1.99 With unknown physiological acceptors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)