Characterization of Porphobilinogen Synthase from an Aerobic Photosynthetic Bacterium, Erythrobacter sp. Strain Och 114
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概要
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Porphobilinogen synthase (formerly 5-aminolevulinic acid dehydratase, EC 4.2.1.24) was purified 7,405-fold from an aerobic photosynthetic bacterium, Erythrobacter sp. strain OCh 114. The molecular weight of the enzyme was determined to be 260,000 by Sephadex G-200 gel filtration. The enzyme had a single pH optimum at 8.0 and showed no requirement for metal ion and thiol compound for its maximum activity. The K_m value for 5-aminolevulinic acid was 0.29 mM. 4,5-Dioxovaleric acid and levulinic acid were found to be competitive inhibitors of the enzyme, with K_i values of 0.65 and 0.80 mM, respectively. The enzyme was extremely labile in acidic pH and almost completely lost its activity within 1 h at pH 6.0 and 30℃. This Erythrobacter enzyme seems to be similar to the enzyme from the anaerobic photosynthetic bacterium Rhodobacter capsulatus in its molecular and catalyiic properties.
- 日本植物生理学会の論文
著者
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Shioi Yuzo
Division Of Biology Miyazaki Medical College
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Doi M
Division Of Biology Miyazaki Medical College
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Doi Michio
Division Of Biology Miyazaki Medical College
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