Premium
Enzymatic characterization of peroxisomal and cytosolic betaine aldehyde dehydrogenases in barley
Author(s) -
Fujiwara Takashi,
Hori Kazuya,
Ozaki Keiko,
Yokota Yuka,
Mitsuya Shiro,
Ichiyanagi Tsuyoshi,
Hattori Tasuku,
Takabe Tetsuko
Publication year - 2008
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.2008.01122.x
Subject(s) - betaine , biochemistry , glycine , chemistry , hordeum vulgare , enzyme , aldehyde dehydrogenase , aldehyde , peroxisome , biology , amino acid , gene , botany , poaceae , catalysis
Betaine aldehyde dehydrogenase (BADH; EC 1.2.1.8) is an important enzyme that catalyzes the last step in the synthesis of glycine betaine, a compatible solute accumulated by many plants under various abiotic stresses. In barley ( Hordeum vulgare L.), we reported previously the existence of two BADH genes ( BBD1 and BBD2 ) and their corresponding proteins, peroxisomal BADH (BBD1) and cytosolic BADH (BBD2). To investigate their enzymatic properties, we expressed them in Escherichia coli and purified both proteins. Enzymatic analysis indicated that the affinity of BBD2 for betaine aldehyde was reasonable as other plant BADHs, but BBD1 showed extremely low affinity for betaine aldehyde with apparent K m of 18.9 μ M and 19.9 m M , respectively. In addition, V max /K m with betaine aldehyde of BBD2 was about 2000‐fold higher than that of BBD1, suggesting that BBD2 plays a main role in glycine betaine synthesis in barley plants. However, BBD1 catalyzed the oxidation of ω‐aminoaldehydes such as 4‐aminobutyraldehyde and 3‐aminopropionaldehyde as efficiently as BBD2. We also found that both BBDs oxidized 4‐ N ‐trimethylaminobutyraldehyde and 3‐ N ‐trimethylaminopropionaldehyde.