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OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes
Author(s) -
Mitsuya Shiro,
Yokota Yuka,
Fujiwara Takashi,
Mori Nobuhiro,
Takabe Tetsuko
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.10.039
Subject(s) - peroxisome , oryza sativa , acetaldehyde , aldehyde dehydrogenase , betaine , catalase , biochemistry , glycine , chemistry , photorespiration , gene , enzyme , amino acid , ethanol
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.