OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes |
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| Authors: | Shiro Mitsuya Takashi Fujiwara Tetsuko Takabe |
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| Affiliation: | a Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan
b United Graduate School of Bioagricultural Sciences, Tottori University, Koyama, Tottori 680-8550, Japan |
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| 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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| Keywords: | AB-ald, 4-aminobutyraldehyde ADH, alcohol dehydrogenase ALDH, aldehyde dehydrogenase AP-ald, 3-aminopropionaldehyde BADH, betaine aldehyde dehydrogenase CAT, catalase GB, glycine betaine mRFP, monomeric red fluorescent protein PDC, pyruvate decarboxylase SKL, Ser-Lys-Leu SRL, Ser-Arg-Leu TMAB-ald, 4-N-trimethylaminobutyraldehyde TMAP-ald, 3-N-trimethylaminopropionaldehyde |
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