Abstract
The recently cloned and characterized human polyamine oxidase (PAOhl) potentially represents a new class of catabolic enzymes in the mammalian polyamine metabolic pathway capable of the efficient oxidation of polyamines. Here the discovery of three additional human PAO splice variants is reported, and the data support the fact that the human PAO gene codes for at least four isoenzymes, each of which exhibit distinctive biochemical characteristics, suggesting the existence of additional levels of complexity in polyamine catabolism.
Original language | English (US) |
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Pages (from-to) | 673-677 |
Number of pages | 5 |
Journal | Biochemical Journal |
Volume | 368 |
Issue number | 3 |
DOIs | |
State | Published - Dec 15 2002 |
Keywords
- Isoform
- N-acetylspermine
- Polyamines
- Spermidine
- Spermine
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology