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Your query returned 4 entries. Printable version
EC | 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) | ||||||||
Comments: | 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). | ||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||
References: |
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EC | 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 |
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Other name(s): | polyamine oxidase (ambiguous); Fms1; AtPAO3 | ||||||||
Systematic name: | polyamine:oxygen oxidoreductase (3-aminopropanal or 3-acetamidopropanal-forming) | ||||||||
Comments: | 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). | ||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||
References: |
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EC | 2.5.1.126 | ||||||||
Accepted name: | norspermine synthase | ||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + norspermidine = S-methyl-5′-thioadenosine + norspermine | ||||||||
Glossary: | norspermidine = bis(3-aminopropyl)amine norspermine = N,N′-bis(3-aminopropyl)-1,3-propanediamine spermidine = N-(3-aminopropyl)-1,4-butanediamine thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine |
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Other name(s): | long-chain polyamine synthase (ambiguous) | ||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:norspermidine 3-aminopropyltransferase | ||||||||
Comments: | The enzyme, characterized from the thermophilic archaeon Pyrobaculum aerophilum, can also synthesize norspermidine from propane-1,3-diamine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.127, caldopentamine synthase, this enzyme does not accept norspermine as a substrate. | ||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc, PDB | ||||||||
References: |
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EC | 2.5.1.127 | ||||||||
Accepted name: | caldopentamine synthase | ||||||||
Reaction: | S-adenosyl 3-(methylsulfanyl)propylamine + norspermine = S-methyl-5′-thioadenosine + caldopentamine | ||||||||
Glossary: | caldopentamine = N-(3-aminopropyl)-N′-{3-[(3-aminopropyl)amino]propyl}-1,3-propanediamine norspermidine = N-(3-aminopropyl)-1,4-butanediamine norspermine = N,N′-bis(3-aminopropyl)-1,3-propanediamine spermidine = N-(3-aminopropyl)-1,4-butanediamine thermospermine = N-{3-[(3-aminopropyl)amino]propyl}-1,4-butanediamine |
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Other name(s): | long-chain polyamine synthase (ambiguous) | ||||||||
Systematic name: | S-adenosyl 3-(methylsulfanyl)propylamine:norspermine 3-aminopropyltransferase | ||||||||
Comments: | The enzyme, characterized from the thermophilic archaeon Hyperthermus butylicus, can also synthesize norspermine from norspermidine and thermospermine from spermidine (with lower activity). The long-chain polyamines stabilize double-stranded DNA at high temperatures. In contrast to EC 2.5.1.23, sym-norspermidine synthase and EC 2.5.1.126, norspermine synthase, this enzyme shows no activity with propane-1,3-diamine. | ||||||||
Links to other databases: | BRENDA, EXPASY, KEGG, MetaCyc | ||||||||
References: |
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