| Literature DB >> 12736784 |
Jeyanthi Rebecca Livingstone1, Toshiya Maruo, Izumi Yoshida, Yutaka Tarui, Kiyoo Hirooka, Yoshihiro Yamamoto, Nobuo Tsutui, Eiji Hirasawa.
Abstract
Betaine aldehyde dehydrogenase (BADH; EC 1.2.1.8) is the enzyme that catalyzes the second step in the synthesis of the osmoprotectant, glycine betaine. NAD-dependent BADH was purified from Avena sativa shoots by DEAE Sephacel, hydroxyapatite, 5'-AMP Sepharose 4B, Mono Q and TSK-GEL column chromatographies to homogeneity by the criterion of native PAGE, and the properties of BADH were compared with those of aminoaldehyde dehydrogenase purified to homogeneity from A. sativa. The molecular mass estimated by both gel filtration using TSK-GEL column and Sephacryl S-200 was 120 and 115, kDa, respectively. The enzyme is a homodimer with a subunit molecular mass of 61 kDa as shown by SDS-PAGE. The pI value of the enzyme was found to be 6.3. The purified enzyme catalyzed not only the oxidation of betaine aldehyde (BAL), but also that of aminoaldehydes, 3-aminopropionaldehyde (APAL), 4-aminobutyraldehyde (ABAL), and 4-guanidinobutyraldehyde (GBAL). The K(m) values for BAL, APAL, ABAL and GBAL were 5x10(-6), 5.4x10(-7), 2.4x10(-5) and 5x10(-5) M, respectively. APAL showed substrate inhibition at a concentration of 0.1 mM. A fragment of BADH cleaved by V8 protease shared homology with other plant BADHs.Entities:
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Year: 2003 PMID： 12736784 DOI： 10.1007/s10265-003-0077-7
Source DB: PubMed Journal: J Plant Res ISSN： 0918-9440 Impact factor: 2.629