Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics

Tracy Murray Stewart, Yanlin Wang, Wendy Devereux, Robert A Casero

Research output: Contribution to journalArticle

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 languageEnglish (US)
Pages (from-to)673-677
Number of pages5
JournalBiochemical Journal
Volume368
Issue number3
DOIs
StatePublished - Dec 15 2002

Fingerprint

Cloning
Polyamines
Isoenzymes
Organism Cloning
Metabolic Networks and Pathways
Genes
Oxidation
Enzymes
polyamine oxidase

Keywords

  • Isoform
  • N-acetylspermine
  • Polyamines
  • Spermidine
  • Spermine

ASJC Scopus subject areas

  • Biochemistry

Cite this

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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.",
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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.

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