Enzymes
| UniProtKB help_outline | 2 proteins |
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| GO Molecular Function help_outline |
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- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N8-acetylspermidine Identifier CHEBI:58535 Charge 2 Formula C9H23N3O InChIKeyhelp_outline FONIWJIDLJEJTL-UHFFFAOYSA-P SMILEShelp_outline CC(=O)NCCCC[NH2+]CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline O2 Identifier CHEBI:15379 (CAS: 7782-44-7) help_outline Charge 0 Formula O2 InChIKeyhelp_outline MYMOFIZGZYHOMD-UHFFFAOYSA-N SMILEShelp_outline O=O 2D coordinates Mol file for the small molecule Search links Involved in 2,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-acetamidobutanal Identifier CHEBI:7386 (Beilstein: 1925525) help_outline Charge 0 Formula C6H11NO2 InChIKeyhelp_outline DDSLGZOYEPKPSJ-UHFFFAOYSA-N SMILEShelp_outline [H]C(=O)CCCNC(C)=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O2 Identifier CHEBI:16240 (Beilstein: 3587191; CAS: 7722-84-1) help_outline Charge 0 Formula H2O2 InChIKeyhelp_outline MHAJPDPJQMAIIY-UHFFFAOYSA-N SMILEShelp_outline [H]OO[H] 2D coordinates Mol file for the small molecule Search links Involved in 426 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline propane-1,3-diamine Identifier CHEBI:57484 Charge 2 Formula C3H12N2 InChIKeyhelp_outline XFNJVJPLKCPIBV-UHFFFAOYSA-P SMILEShelp_outline [NH3+]CCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:25972 | RHEA:25973 | RHEA:25974 | RHEA:25975 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Yeast Fms1 is a FAD-utilizing polyamine oxidase.
Landry J., Sternglanz R.
In this report we show that recombinant Saccharomyces cerevisiae Fms1 protein is a polyamine oxidase that binds FAD with an FAD:Fms1 stoichiometry of 1:1. Biochemical characterization of Fms1 shows that it can oxidize spermine, N(1)-acetylspermine, N(1)-acetylspermidine, and N(8)-acetylspermidine, ... >> More
In this report we show that recombinant Saccharomyces cerevisiae Fms1 protein is a polyamine oxidase that binds FAD with an FAD:Fms1 stoichiometry of 1:1. Biochemical characterization of Fms1 shows that it can oxidize spermine, N(1)-acetylspermine, N(1)-acetylspermidine, and N(8)-acetylspermidine, but not spermidine. The products of spermine oxidation are spermidine and 3-aminopropanal. A kinetic analysis revealed that spermine, N(1)-acetylspermine, and N(1)-acetylspermidine are oxidized with similar efficiencies, while N(8)-acetylspermidine is a poor substrate. The data support a previous report, suggesting that Fms1 is responsible for the production of beta-alanine from spermine for the synthesis of pantothenic acid. << Less
Biochem. Biophys. Res. Commun. 303:771-776(2003) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.
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Polyamine oxidase from Acanthamoeba culbertsoni specific for N8-acetylspermidine.
Shukla O.P., Muller S., Walter R.D.
Polyamine oxidase plays a key role in the catabolism of polyamines and regeneration of spermidine and putrescine. The mammalian enzyme utilises N1-acetylspermidine, and N8-acetylspermidine, although formed in the mammals, is not catabolised further. We have characterised an enzyme from Acanthamoeb ... >> More
Polyamine oxidase plays a key role in the catabolism of polyamines and regeneration of spermidine and putrescine. The mammalian enzyme utilises N1-acetylspermidine, and N8-acetylspermidine, although formed in the mammals, is not catabolised further. We have characterised an enzyme from Acanthamoeba culbertsoni which acts preferentially on N8-acetylspermidine. The highly unstable enzyme was stabilised in the presence of glycerol or dimethylsulphoxide together with spermine and purified 400-fold by a combination of DEAE-cellulose, CM-cellulose, spermine-Sepharose and Sephacryl S-300 chromatography. The enzyme has a pH optimum of 8 and a temperature optimum of 45 degrees C. The relative activities on different substrates are: N8-acetylspermidine 100%, N1-acetylspermine 40%, N1-acetylspermidine 1%, N1,8-diacetylspermidine 1% and N1,12-diacetylspermine 15%. Free polyamines and substrates of monoamine oxidase were not attacked. The enzyme yielded diaminopropane as an end product of catabolism and could be involved in the biosynthesis of this unusual polyamine present in large amounts in this organism. << Less