Purification and properties of aminoaldehyde dehydrogenase from <Emphasis Type="Italic">Avena</Emphasis><Emphasis Type="Italic">sativa</Emphasis> |
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Authors: | Jeyanthi Livingstone Izumi Yoshida Yutaka Tarui Kiyoo Hirooka Yoshihiro Yamamoto Nobuo Tsutui Eiji Hirasawa |
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Institution: | (1) Division of Bio- and Geosciences, Graduate School of Science, Osaka City University, Sumiyoshi-ku, Osaka 558-8585, Japan,;(2) Kyoto Municipal Institute for Industrial Research, Kyoto Research Park, Shimogyo-ku, Kyoto 600-8813, Japan, |
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Abstract: | NAD-dependent aminoaldehyde dehydrogenase (AMADH, EC 1.2.1.-) from Avena shoots was purified by DEAE Sephacel, hydroxyapatite, 5′-AMP Sepharose 4B, Mono Q, and TSK-GEL column chromatographies to
homogeneity by the criterion of native PAGE. SDS–PAGE yielded a single band at a molecular mass of 55 kDa. IEF studies showed
a band with a pI value of 5.3. In contrast to AMADHs from other species, the TSK-GEL chromatography showed that Avena AMADH exists as a monomer in the native state. The purified enzyme catalyzed the oxidations of 3-aminopropionaldehyde (APAL),
4-aminobutyraldehyde (ABAL) N-(3-aminopropyl)-4-aminobutyraldehyde (APBAL), and 4-guanidinobutyraldehyde (GBAL), but not of betaine aldehyde or indoleacetaldehyde.
The K
m values for APAL, ABAL, and GBAL were 1.5×10–6, 2.2×10–6, and 1.3×10–5 M, respectively. Although N-terminal amino acid sequence of Avena AMADH could not be determined due to a modification of the amino residue, the sequence of the fragment of AMADH cleaved by
V8 protease showed greater similarity to the barley BADH than to the pea AMADH.
Electronic Publication |
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Keywords: | 3-Aminopropionaldehyde 4-Aminobutyraldehyde Aminoaldehyde dehydrogenase Monomer structure |
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