3-Hydroxyisobutyrate Dehydrogenase from Pseudomonas putida E23: Purification and Characterization
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概要
- 論文の詳細を見る
The NAD^+-dependent 3-hydroxyisobutyrate dehydrogenase [EC 1.1.1.31] was purified to homogeneity from Pseudomonas putida E23. The enzyme was a tetramer (molecular mass, 120 kDa) consisted of identical subunits (molecular mass, 30 kDa). The enzyme was specific for NAD^+ (K_m, 0.44 mM). The maximal activity was obtained at about pH 10. The enzyme was specific for the L-isomer of 3-hydroxyisobutyrate. In addition to L-3-hydroxyisobutyrate, L-serine, 2-methyl-DL-serine, and 3-hydroxypropionate were substrates. The K_m for L-3-hydroxyisobutyrate, L-serine, 2-methyl-DL-serine, and 3-hydroxypropionate were 0.12, 18, 44, and 83 mM, respectively. The enzyme was inhibited by p-chloromercuribenzoate, HgCl_2, and AgNO_3, but not by EDTA, α,α'-dipyridyl, and o-phenanthroline. The N-terminal 26 amino acid sequence was compared with the sequences deduced from the enzyme genes of rat liver and Pseudomonas aeruginosa.
- 社団法人日本農芸化学会の論文
- 1996-12-23
著者
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Chowdhury E
Department Of Bioresources Science Kochi University:(present Address)department Of Biochemistry Univ
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Misono H
Kochi Univ. Kochi Jpn
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Misono Haruo
Department Of Bioresources Science Faculty Of Agriculture Kochi University
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Misono Haruo
Department Of Bioresource Science Kochi University
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Misono Haruo
Laboratory Of Applied Microbiology Department Of Agricultural Chemistry Kochi University
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NAGATA Shinji
Laboratory of Bioorganic Chemistry, Department of Applied Biological Chemistry, Graduate School of A
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Chowdhury Emran
Laboratory of Applied Microbiology, Department of Bioresources Science, Kochi University
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Nagata S
Department Of Bioresources Science Kochi University
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Nagata Shinji
Laboratory Of Applied Microbiology Department Of Bioresources Science Kochi University
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