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Microbiology 152 (2006), 2265-2272; DOI  10.1099/mic.0.28920-0
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Microbiology 152 (2006), 2265-2272; DOI  10.1099/mic.0.28920-0
© 2006 Society for General Microbiology

Characterization and a role of Pseudomonas aeruginosa spermidine dehydrogenase in polyamine catabolism

Veeranki Venkata Dasu1,{dagger}, Yuji Nakada1,{ddagger}, Mayumi Ohnishi-Kameyama1, Keitarou Kimura1 and Yoshifumi Itoh1,2

1 National Food Research Institute, Kannondai 2-1-12, Tsukuba, Ibaraki 305-8642, Japan
2 Akita Research Institute for Food and Brewing, Sanuki 4-26, Araya-machi, Akita 010-1623, Japan

Correspondence
Yoshifumi Itoh
yosifumi{at}arif.pref.akita.jp

Pseudomonas aeruginosa PAO1 has two possible catabolic pathways of spermidine and spermine; one includes the spuA and spuB products with unknown functions and the other involves spermidine dehydrogenase (SpdH; EC 1.5.99.6) encoded by an unknown gene. The properties of SpdH in P. aeruginosa PAO1 were characterized and the corresponding spdH gene in this strain identified. The deduced SpdH (620 residues, calculated Mr of 68 861) had a signal sequence of 28 amino acids at the amino terminal and a potential transmembrane segment between residues 76 and 92, in accordance with membrane location of the enzyme. Purified SpdH oxidatively cleaved spermidine into 1,3-diaminopropane and 4-aminobutyraldehyde with a specific activity of 37 units (mg protein)–1 and a Km value of 36 µM. The enzyme also hydrolysed spermine into spermidine and 3-aminopropanaldehyde with a specific activity of 25 units (mg protein)–1 and a Km of 18 µM. Knockout of spdH had no apparent effect on the utilization of both polyamines, suggesting that this gene is minimally involved in polyamine catabolism. However, when spdH was fused to the polyamine-inducible promoter of spuA, it fully restored the ability of a spuA mutant to utilize spermidine. It is concluded that SpdH can perform a catabolic role in vivo, but P. aeruginosa PAO1 does not produce sufficient amounts of the enzyme to execute this function.


Two supplementary figures are available with the online version of this paper.

{dagger}Present address: Department of Biotechnology, Indian Institute of Technology-Guwahati, North Guwahati, Guwahati-781039, Assam, India.

{ddagger}Present address: Department of Nursing, Faculty of Nursing and Rehabilitation, Aino University, Higashiohda 4-5-4, Ibaraki, Osaka 567-0012, Japan.







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