- Information
- Symbol: BAD1,OsBADH1
- MSU: LOC_Os04g39020
- RAPdb: Os04g0464200
- Publication
- OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes, 2009, FEBS Lett.
- Dissecting substrate specificity of two rice BADH isoforms: Enzyme kinetics, docking and molecular dynamics simulation studies, 2012, Biochimie.
- Genetic manipulation of Japonica rice using the OsBADH1 gene from Indica rice to improve salinity tolerance, 2010, Plant Cell, Tissue and Organ Culture (PCTOC).
- Expression of OsBADH1 gene in Indica rice Oryza sativaL. in correlation with salt, plasmolysis, temperature and light stresses , 2011, Plant Omics.
- Inactivation of an aminoaldehyde dehydrogenase is responsible for fragrance in rice, 2008, Plant Mol Biol.
- Expression of Indica rice OsBADH1 gene under salinity stress in transgenic tobacco, 2009, Plant Biotechnology Reports.
- RNAi-directed downregulation of betaine aldehyde dehydrogenase 1 OsBADH1 results in decreased stress tolerance and increased oxidative markers without affecting glycine betaine biosynthesis in rice Oryza sativa., 2014, Plant Mol Biol.
- Resequencing Reveals Different Domestication Rate for BADH1 and BADH2 in Rice Oryza sativa., 2015, PLoS One.
- Genbank accession number
- Key message
- Northern blot analysis revealed that salt-tolerant in each rice cultivar is correlated to the expression level of OsBADH1 mRNA
- Moreover, these results suggest that the expression of OsBADH1 gene in response to salt stress could be magnified under high light conditions
- Interestingly, the effect of salt stress on the expression of OsBADH1 gene was alleviated by CO2 enrichment
- Expression of OsBADH1 gene in Indica rice (Oryza sativaL.) in correlation with salt, plasmolysis, temperature and light stresses
- We previously found that the expression of betaine aldehyde dehydrogenase 1 gene (OsBADH1), encoding a key enzyme for glycine betaine biosynthesis pathway, showed close correlation with salt tolerance of rice
- In this study, the expression of the OsBADH1 gene in transgenic tobacco was investigated in response to salt stress using a transgenic approach
- The expression studies showed that OsBADH1 can be induced by a variety of environmental factors such as salinity, drought, cold, heat, light intensity and CO2 concentration
- The results demonstrated that the OsBADH1 mRNA expression was up-regulated by salinity, drought, cold and high light intensity but down-regulated by CO2 enrichment and heat stress
- The primary response of OsBADH1 gene expression was induced within 24 h after salinity, cold or drought stress treatment
- Expression of Indica rice OsBADH1 gene under salinity stress in transgenic tobacco
- Japonica rice (salt-sensitive) was genetically engineered to enhance salt tolerance by introducing the OsBADH1 gene from Indica rice (salt-tolerant), which is a GB accumulator
- Genetic manipulation of Japonica rice using the OsBADH1 gene from Indica rice to improve salinity tolerance
- The accumulation of OsBADH1 mRNA decreases following submergence treatment, but quickly recovers after re-aeration
- Transgenic rice lines downregulating OsBADH1 exhibited remarkably reduced tolerance to NaCl, drought and cold stresses
- In this study, we demonstrated a pivotal role of OsBADH1 in stress tolerance without altering GB biosynthesis capacity, using the RNA interference (RNAi) technique
- Connection
- BAD1~OsBADH1, OsBADH2~fgr, OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes, We found that OsBADH1 catalyzes the oxidation of acetaldehyde efficiently, while the activity of OsBADH2 is extremely low
- BAD1~OsBADH1, OsBADH2~fgr, Dissecting substrate specificity of two rice BADH isoforms: Enzyme kinetics, docking and molecular dynamics simulation studies, Fragrance rice (Oryza sativa) contains two isoforms of BADH, named OsBADH1 and OsBADH2
- BAD1~OsBADH1, OsBADH2~fgr, Dissecting substrate specificity of two rice BADH isoforms: Enzyme kinetics, docking and molecular dynamics simulation studies, OsBADH1 is implicated in acetaldehyde oxidation in rice plant peroxisomes, while the non-functional OsBADH2 is believed to be involved in the accumulation of 2-acetyl-1-pyrroline, the major compound of aroma in fragrance rice
- BAD1~OsBADH1, OsBADH2~fgr, Dissecting substrate specificity of two rice BADH isoforms: Enzyme kinetics, docking and molecular dynamics simulation studies, Consistent with our previous study, kinetics data indicated that the enzymes catalyze the oxidation of GAB-ald more efficiently than Bet-ald and the OsBADH1 W172F and OsBADH2 W170F mutants displayed a higher catalytic efficiency towards GAB-ald
- BAD1~OsBADH1, OsBADH2~fgr, Dissecting substrate specificity of two rice BADH isoforms: Enzyme kinetics, docking and molecular dynamics simulation studies, The amino acid residues, E262, L263, C296 and W461 of OsBADH1 and E260, L261, C294 and W459 of OsBADH2 located within 5 A of the OsBADH active site mainly interacted with GAB-ald forming strong hydrogen bonds in both OsBADH isoforms
- BAD1~OsBADH1, OsBADH2~fgr, Dissecting substrate specificity of two rice BADH isoforms: Enzyme kinetics, docking and molecular dynamics simulation studies, Residues W163, N164, Q294, C296 and F397 of OsBADH1-Bet-ald and Y163, M167, W170, E260, S295 and C453 of OsBADH2-Bet-ald formed the main interaction sites while E260 showed an interaction energy of -14
- BAD1~OsBADH1, OsBADH2~fgr, Dissecting substrate specificity of two rice BADH isoforms: Enzyme kinetics, docking and molecular dynamics simulation studies, Unconserved A290 in OsBADH1 and W288 in OsBADH2 appeared to be important for substrate recognition similar to that observed in PsAMADHs
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