Journal
PROTEIN JOURNAL
Volume 30, Issue 8, Pages 529-538Publisher
SPRINGER
DOI: 10.1007/s10930-011-9358-5
Keywords
Betaine aldehyde dehydrogenase; Kinetics; Oryza sativa
Categories
Funding
- Faculty of Science, Kasetsart University
- Commission on Higher Education
- Agricultural Research Development Agency (public organization), Thailand
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Betaine aldehyde dehydrogenase 2 (BADH2) is believed to be involved in the accumulation of 2-acetyl-1-pyrroline (2AP), one of the major aromatic compounds in fragrant rice. The enzyme can oxidize omega-aminoaldehydes to the corresponding omega-amino acids. This study was carried out to investigate the function of wild-type BADHs and four BADH2 mutants: BADH2_Y420, containing a Y420 insertion similar to BADH2.8 in Myanmar fragrance rice, BADH2_C294A, BADH2_E260A and BADH2_N162A, consisting of a single catalytic-residue mutation. Our results showed that the BADH2_Y420 mutant exhibited less catalytic efficiency towards gamma-aminobutyraldehyde but greater efficiency towards betaine aldehyde than wild-type. We hypothesized that this point mutation may account for the accumulation of gamma-aminobutyraldehyde/Delta(1)-pyrroline prior to conversion to 2AP, generating fragrance in Myanmar rice. In addition, the three catalytic-residue mutants confirmed that residues C294, E260 and N162 were involved in the catalytic activity of BADH2 similar to those of other BADHs.
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