Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics
- 15 December 2002
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 368 (3) , 673-677
- https://doi.org/10.1042/bj20021587
Abstract
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.Keywords
This publication has 19 references indexed in Scilit:
- Identification and characterization of a novel flavin-containing spermine oxidase of mammalian cell originBiochemical Journal, 2002
- Detoxification of the polyamine analogue N1-ethyl-N11-[(cycloheptyl)methy]-4,8-diazaundecane (CHENSpm) by polyamine oxidase.2002
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded ProteinScience, 2002
- Apoptotic signaling in polyamine analogue-treated SK-MEL-28 human melanoma cells.2001
- Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure.2001
- Protein translocation machineries of peroxisomesFEBS Letters, 2001
- A barley polyamine oxidase isoform with distinct structural features and subcellular localizationEuropean Journal of Biochemistry, 2001
- Terminally Alkylated Polyamine Analogues as Chemotherapeutic AgentsJournal of Medicinal Chemistry, 2000
- Primary structure and expression of peroxisomal acetylspermidine oxidase in the methylotrophic yeast Candida boidiniiFEBS Letters, 2000
- A 30 Å long U-shaped catalytic tunnel in the crystal structure of polyamine oxidaseStructure, 1999