| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10872185 | FEBS Letters | 2009 | 5 Pages |
Abstract
Although rice (Oryza sativa L.) produces little glycine betaine (GB), it has two betaine aldehyde dehydrogenase (BADH; EC 1.2.1.8) gene homologs (OsBADH1 and OsBADH2). We found that OsBADH1 catalyzes the oxidation of acetaldehyde efficiently, while the activity of OsBADH2 is extremely low. The accumulation of OsBADH1 mRNA decreases following submergence treatment, but quickly recovers after re-aeration. We confirmed that OsBADH1 localizes in peroxisomes. In this paper, a possible physiological function of OsBADH1 in the oxidation of acetaldehyde produced by catalase in rice plant peroxisomes is discussed.
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Agricultural and Biological Sciences
Plant Science
Authors
Shiro Mitsuya, Yuka Yokota, Takashi Fujiwara, Nobuhiro Mori, Tetsuko Takabe,