Non-specific polyamine oxidase

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Non-specific polyamine oxidase
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EC no. 1.5.3.17
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Non-specific polyamine oxidase (EC 1.5.3.17, polyamine oxidase, Fms1, AtPAO3) is an enzyme with systematic name polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming). [1] [2] [3] This enzyme catalyses the following chemical 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

This enzyme is flavoprotein (FAD).

Related Research Articles

Spermine is a polyamine involved in cellular metabolism that is found in all eukaryotic cells. The precursor for synthesis of spermine is the amino acid ornithine. It is an essential growth factor in some bacteria as well. It is found as a polycation at physiological pH. Spermine is associated with nucleic acids and is thought to stabilize helical structure, particularly in viruses. It functions as an intracellular free radical scavenger to protect DNA from free radical attack. Spermine is the chemical primarily responsible for the characteristic odor of semen.

In enzymology, a thiamine oxidase (EC 1.1.3.23) is an enzyme that catalyzes the chemical reaction

In enzymology, an abscisic-aldehyde oxidase (EC 1.2.3.14) is an enzyme that catalyzes the chemical reaction

In enzymology, an indole-3-acetaldehyde oxidase (EC 1.2.3.7) is an enzyme that catalyzes the chemical reaction

In enzymology, a D-aspartate oxidase (EC 1.4.3.1) is an enzyme that catalyzes the chemical reaction

A polyamine oxidase (PAO) is an enzymatic flavoprotein that oxidizes a carbon-nitrogen bond in a secondary amino group of a polyamine donor, using molecular oxygen as an acceptor. The generalized PAO reaction converts three substrates into three products. Different PAOs with varying substrate specificities exist in different organisms. Phylogenetic analyses suggest that PAOs likely evolved once in eukaryotes and diversified by divergent evolution and gene duplication events, though some prokaryotes have acquired PAOs through horizontal gene transfer.

In enzymology, a prenylcysteine oxidase (EC 1.8.3.5) is an enzyme that catalyzes the chemical reaction

In enzymology, a putrescine oxidase (EC 1.4.3.10) is an enzyme that catalyzes the chemical reaction

In enzymology, a (S)-6-hydroxynicotine oxidase (EC 1.5.3.5) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">SAT1 (gene)</span> Protein-coding gene in the species Homo sapiens

Diamine acetyltransferase 1 is an enzyme that in humans is encoded by the SAT1 gene found on the X chromosome.

<span class="mw-page-title-main">SMOX</span> Enzyme

Spermine oxidase is an enzyme that in humans is encoded by the SMOX gene.

<span class="mw-page-title-main">Glycine oxidase</span> Class of enzymes

Glycine oxidase (EC 1.4.3.19) is an enzyme with systematic name glycine:oxygen oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction

Pseudooxynicotine oxidase (EC 1.4.3.24) is an enzyme with systematic name 4-(methylamino)-1-(pyridin-3-yl)butan-1-one:oxygen oxidoreductase (methylamine releasing). This enzyme catalyses the following chemical reaction

N1-acetylpolyamine oxidase (EC 1.5.3.13, hPAO-1, mPAO, hPAO) is an enzyme with systematic name N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming). This enzyme catalyses the following chemical reaction

Polyamine oxidase (propane-1,3-diamine-forming) (EC 1.5.3.14, MPAO, maize PAO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (propane-1,3-diamine-forming). This enzyme catalyses the following chemical reaction

N8-acetylspermidine oxidase (propane-1,3-diamine-forming) (EC 1.5.3.15) is an enzyme with systematic name N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming). This enzyme catalyses the following chemical reaction

Spermine oxidase (EC 1.5.3.16, PAOh1/SMO, AtPAO1, AtPAO4, SMO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (spermidine-forming). This enzyme catalyses the following chemical reaction

Farnesylcysteine lyase (EC 1.8.3.6, FC lyase, FCLY) is an enzyme with systematic name S-(2E,6E)-farnesyl-L-cysteine oxidase. This enzyme catalyses the following chemical reaction

Ent-kaurene oxidase (EC 1.14.14.86, Formerly EC 1.14.13.78) is an enzyme with systematic name ent-kaur-16-ene,NADPH:oxygen oxidoreductase (hydroxylating). This enzyme catalyses the following chemical reaction

Homospermidine synthase (EC 2.5.1.44) is an enzyme with systematic name putrescine:putrescine 4-aminobutyltransferase (ammonia-forming). This enzyme catalyses the following chemical reaction

References

  1. ↑ Moschou PN, Sanmartin M, Andriopoulou AH, Rojo E, Sanchez-Serrano JJ, Roubelakis-Angelakis KA (August 2008). "Bridging the gap between plant and mammalian polyamine catabolism: a novel peroxisomal polyamine oxidase responsible for a full back-conversion pathway in Arabidopsis". Plant Physiology. 147 (4): 1845–57. doi:10.1104/pp.108.123802. PMC   2492618 . PMID   18583528.
  2. ↑ Müller S, Walter RD (April 1992). "Purification and characterization of polyamine oxidase from Ascaris suum". The Biochemical Journal. 283 ( Pt 1): 75–80. PMC   1130995 . PMID   1567380.
  3. ↑ Landry J, Sternglanz R (April 2003). "Yeast Fms1 is a FAD-utilizing polyamine oxidase". Biochemical and Biophysical Research Communications. 303 (3): 771–6. doi:10.1016/s0006-291x(03)00416-9. PMID   12670477.
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