期刊
PLANT PHYSIOLOGY AND BIOCHEMISTRY
卷 119, 期 -, 页码 159-169出版社
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.plaphy.2017.08.018
关键词
Back-conversion reaction; Homology modeling; Polyamine oxidase; Phylogenetic tree analysis; Synechocystis
资金
- Chulalongkorn University Dutsadi Phiphat Scholarship
- Chulalongkorn University Graduate Scholarship
- 90th Anniversary scholarship
- CU Ratchadaphiseksomphote Endowment Fund (Food and Water cluster) [CU-58-011-FW]
- Thailand Research Fund [IRG578008]
The intracellular polyamine contents are regulated not only by polyamine biosynthesis and transport but also by polyamine degradation catalyzed by copper-dependent amine oxidase (DAO) and FAD-dependent polyamine oxidase (PAO). The genome sequence of Synechocystis sp. PCC 6803 reveals the presence of at least one putative polyamine oxidase gene, slr5093. The open reading frame of slr5093 encoding Synechocystis polyamine oxidase (SynPAO, E.C. 1.5.3.17) was expressed in Escherichia coli. The purified recombinant enzyme had the characteristic absorption spectrum of a flavoprotein with absorbance peaks at 380 and 450 nm. The optimum pH and temperature for the oxidation of both spermidine and spermine are 8.5 and 30 degrees C, respectively. The enzyme catalyzed the conversion of spermine and spermidine to spermidine and putrescine, respectively, with higher catalytic efficiency when spermine served as substrate. These results suggest that SynPAO is a polyamine oxidase involved in a polyamine back conversion pathway. Based on the structural analysis, Gln94, Tyr403 and Thr440 in SynPAO are predicted to be important residues in the active site. (C) 2017 Elsevier Masson SAS. All rights reserved.
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