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) |
|---|---|
| Pages (from-to) | 673-677 |
| Number of pages | 5 |
| Journal | Biochemical Journal |
| Volume | 368 |
| Issue number | 3 |
| DOIs | |
| State | Published - Dec 15 2002 |
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Keywords
- Isoform
- N-acetylspermine
- Polyamines
- Spermidine
- Spermine
ASJC Scopus subject areas
- Biochemistry
Cite this
Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics. / Murray Stewart, Tracy; Wang, Yanlin; Devereux, Wendy; Casero, Robert A.
In: Biochemical Journal, Vol. 368, No. 3, 15.12.2002, p. 673-677.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics
AU - Murray Stewart, Tracy
AU - Wang, Yanlin
AU - Devereux, Wendy
AU - Casero, Robert A
PY - 2002/12/15
Y1 - 2002/12/15
N2 - 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.
AB - 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.
KW - Isoform
KW - N-acetylspermine
KW - Polyamines
KW - Spermidine
KW - Spermine
UR - http://www.scopus.com/inward/record.url?scp=0037115754&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037115754&partnerID=8YFLogxK
U2 - 10.1042/BJ20021587
DO - 10.1042/BJ20021587
M3 - Article
C2 - 12398765
AN - SCOPUS:0037115754
VL - 368
SP - 673
EP - 677
JO - Biochemical Journal
JF - Biochemical Journal
SN - 0264-6021
IS - 3
ER -