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OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes.
Mitsuya, Shiro; Yokota, Yuka; Fujiwara, Takashi; Mori, Nobuhiro; Takabe, Tetsuko.
Affiliation
  • Mitsuya S; Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
FEBS Lett ; 583(22): 3625-9, 2009 Nov 19.
Article in En | MEDLINE | ID: mdl-19850038
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.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plant Proteins / Oryza / Peroxisomes / Betaine-Aldehyde Dehydrogenase / Acetaldehyde Language: En Journal: FEBS Lett Year: 2009 Document type: Article Affiliation country: Japón Country of publication: Reino Unido

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plant Proteins / Oryza / Peroxisomes / Betaine-Aldehyde Dehydrogenase / Acetaldehyde Language: En Journal: FEBS Lett Year: 2009 Document type: Article Affiliation country: Japón Country of publication: Reino Unido