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EC 1.5.3.16 Details

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EC number

1.5.3.16

Accepted name

spermine oxidase

Reaction

spermine + O₂ + H₂O = spermidine + 3-aminopropanal + H₂O₂

Other name(s)

PAOh1/SMO, PAOh1 (ambiguous), AtPAO1, AtPAO4, SMO, mSMO, SMO(PAOh1), SMO/PAOh1, SMO5, mSMOmu

Systematic name

spermidine:oxygen oxidoreductase (spermidine-forming)

Comment

The enzyme from Arabidopsis thaliana (AtPAO1) oxidizes norspermine to norspermidine with high efficiency [3]. The mammalian enzyme, encoded by the SMOX gene, is a cytosolic enzyme that catalyses the oxidation of spermine at the exo (three-carbon) side of the tertiary amine. No activity with spermidine. Weak activity with N¹-acetylspermine. A flavoprotein (FAD). Differs in specificity from 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 1.5.3.17 (non-specific polyamine oxidase).

History

created 2009

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

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

1.5.1 With NAD⁺ or NADP⁺ as acceptor

1.5.3 With oxygen as acceptor

1.5.3.1 sarcosine oxidase (formaldehyde-forming)

1.5.3.2 N-methyl-L-amino-acid oxidase

1.5.3.3 created 1961, deleted 1972

1.5.3.4 N⁶-methyl-lysine oxidase

1.5.3.5 (S)-6-hydroxynicotine oxidase

1.5.3.6 (R)-6-hydroxynicotine oxidase

1.5.3.7 L-pipecolate oxidase

1.5.3.8 created 1989, deleted 1992

1.5.3.9 created 1989, modified 1999, deleted 2002

1.5.3.10 dimethylglycine oxidase

1.5.3.11 polyamine oxidase

1.5.3.12 dihydrobenzophenanthridine oxidase

1.5.3.13 N¹-acetylpolyamine oxidase

1.5.3.14 polyamine oxidase (propane-1,3-diamine-forming)

1.5.3.15 N⁸-acetylspermidine oxidase (propane-1,3-diamine-forming)

1.5.3.16 spermine oxidase

1.5.3.17 non-specific polyamine oxidase

1.5.3.18 L-saccharopine oxidase

1.5.3.19 4-methylaminobutanoate oxidase (formaldehyde-forming)

1.5.3.20 N-alkylglycine oxidase

1.5.3.21 4-methylaminobutanoate oxidase (methylamine-forming)

1.5.3.22 coenzyme F₄₂₀H₂ oxidase

1.5.3.23 glyphosate oxidoreductase

1.5.3.24 sarcosine oxidase (5,10-methylenetetrahydrofolate-forming)

1.5.3.25 fructosyl amine oxidase (glucosone-forming)

1.5.3.26 fructosyl amine oxidase (fructosamine-forming)

1.5.4 With a disulfide as acceptor

1.5.5 With a quinone or similar compound as acceptor

1.5.7 With an iron-sulfur protein as acceptor

1.5.8 With a flavin or flavoprotein as acceptor

1.5.98 With other, known, physiological acceptors

1.5.99 With unknown physiological acceptors

1.5.99.1 sarcosine dehydrogenase

1.5.99.2 dimethylglycine dehydrogenase

1.5.99.3 L-pipecolate dehydrogenase

1.5.99.4 nicotine dehydrogenase

1.5.99.5 methylglutamate dehydrogenase

1.5.99.6 spermidine dehydrogenase

1.5.99.7 created 1976, deleted 2002

1.5.99.8 proline dehydrogenase

1.5.99.9 methylenetetrahydromethanopterin dehydrogenase

1.5.99.10 created 1999, deleted 2002

1.5.99.11 5,10-methylenetetrahydromethanopterin reductase

1.5.99.12 cytokinin dehydrogenase

1.5.99.13 D-proline dehydrogenase

1.5.99.14 6-hydroxypseudooxynicotine dehydrogenase

1.5.99.15 dihydromethanopterin reductase (acceptor)

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

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

3.1 Acting on ester bonds

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.6 Acting on acid anhydrides

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.10.1 Acting on sulfur-nitrogen bonds (only sub-subclass identified to date)

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)