Publication | Open Access
Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics
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Citations
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References
2002
Year
BiosynthesisAldehyde DehydrogenaseCellular EnzymologyBiochemistryAldo-keto ReductaseNatural SciencesCatabolic EnzymesPolyamine CatabolismBiochemical GeneticsMolecular BiologyMolecular GeneticsDifferent Biochemical CharacteristicsHuman Polyamine OxidaseMedicineEnzymatic ModificationRedox BiologyAlcohol Dehydrogenases
The recently cloned and characterized human polyamine oxidase (PAOh1) 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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