- Information
- Symbol: OsBADH2,fgr
- MSU: LOC_Os08g32870
- RAPdb: Os08g0424500
- PSP score
- LOC_Os08g32870.1: 0.0034
- PLAAC score
- LOC_Os08g32870.1: 0
- pLDDT score
- 97.83
- Protein Structure from AlphaFold and UniProt
- Publication
- Aroma in rice: genetic analysis of a quantitative trait, 1996, Theor Appl Genet.
- 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.
- Haplotype variation at Badh2, the gene determining fragrance in rice, 2012, Genomics.
- RFLP tagging of a gene for aroma in rice, 1992, Theor Appl Genet.
- Characterization of the major fragance gene from an aromatic japonica rice and analysis of its diversity in Asian cultivated rice, 2008, Theor Appl Genet.
- RNAi-directed downregulation of OsBADH2 results in aroma 2-acetyl-1-pyrroline production in rice Oryza sativa L., 2008, BMC Plant Biol.
- Purification, crystallization and preliminary X-ray analysis of recombinant betaine aldehyde dehydrogenase 2 OsBADH2, a protein involved in jasmine aroma, from Thai fragrant rice Oryza sativa L., 2011, Acta Crystallogr Sect F Struct Biol Cryst Commun.
- The gene for fragrance in rice, 2005, Plant Biotechnol J.
- Badh2, encoding betaine aldehyde dehydrogenase, inhibits the biosynthesis of 2-acetyl-1-pyrroline, a major component in rice fragrance, 2008, Plant Cell.
- The origin and evolution of fragrance in rice Oryza sativa L., 2009, Proc Natl Acad Sci U S A.
- Biochemical and enzymatic study of rice BADH wild-type and mutants: an insight into fragrance in rice, 2011, Protein J.
- Inactivation of an aminoaldehyde dehydrogenase is responsible for fragrance in rice, 2008, Plant Mol Biol.
- Creation of fragrant rice by targeted knockout of the OsBADH2 gene using TALEN technology., 2015, Plant Biotechnol J.
- Resequencing Reveals Different Domestication Rate for BADH1 and BADH2 in Rice Oryza sativa., 2015, PLoS One.
- Genbank accession number
- Key message
- RESULTS: The results showed that multiple mutations identical to fgr allele occur in the 13 fragrant rice accessions across China; OsBADH2 is expressed constitutively, with less expression abundance in mature roots; the disrupted OsBADH2 by RNA interference leads to significantly increased 2-acetyl-1-pyrroline production
- 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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