Pathways > spermine and spermidine degradation I
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spermine and spermidine degradation I
Proteins (3)
Protein | Synonyms | Taxonomy |
Peroxisomal N(1)-acetyl-spermine/spermidine oxidase | EC 1.5.3.13; Polyamine oxidase | Mus musculus (house mouse) |
Diamine acetyltransferase 1 | EC 2.3.1.57; Polyamine N-acetyltransferase 1; Putrescine acetyltransferase; Spermidine/spermine N(1)-acetyltransferase 1; SSAT; SSAT-1 | Homo sapiens (human) |
Spermine oxidase | EC 1.5.3.16; Polyamine oxidase 1; PAO-1; PAOh1 | Homo sapiens (human) |
Compounds (11)
Compound | Description |
hydronium ion | |
Hydrogen Peroxide | A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials. |
Water | A clear, odorless, tasteless liquid that is essential for most animal and plant life and is an excellent solvent for many substances. The chemical formula is hydrogen oxide (H2O). (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) |
Oxygen | An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration. |
n(1),n(11)-diethylnorspermine | structure given in first source |
MDL 72527 | RN given refers to di-HCl; RN for parent cpd not available 6/85; polyamine oxidase inhibitor |
Spermidine | A polyamine formed from putrescine. It is found in almost all tissues in association with nucleic acids. It is found as a cation at all pH values, and is thought to help stabilize some membranes and nucleic acid structures. It is a precursor of spermine. |
Coenzyme A | |
Spermine | A biogenic polyamine formed from spermidine. It is found in a wide variety of organisms and tissues and is an essential growth factor in some bacteria. It is found as a polycation at all pH values. Spermine is associated with nucleic acids, particularly in viruses, and is thought to stabilize the helical structure. |
Acetyl Coenzyme A | Acetyl CoA participates in the biosynthesis of fatty acids and sterols, in the oxidation of fatty acids and in the metabolism of many amino acids. It also acts as a biological acetylating agent. |
Flavin-Adenine Dinucleotide | A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972) |