Isolation of Rhizobium leguminosarum biovar viciae Variants with Indole-3-acetamide Hydrolase Activity
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概要
- 論文の詳細を見る
The IAA biosynthetic pathway from tryptophan to IAA via IAM (IAM pathway) was investigated in Rhizobium spp. (fast-growing rhizobium). Southern hybridization with the bam gene, a structural gene for IAM hydrolase (the enzyme that converts IAM to IAA) cloned from Bradyrhizobium japonicum J 1063, indicated that homologous sequences exist among wild-type Rhizobium spp. However the IAM pathway has not been detected biochemically in free-living bacteria. When 5-methyltryptophan-resistant strains were screened for Rhizobium leguminosarum biovar viciae K5 which has DNA sequences with high homology to the bam gene, spontaneous mutants showing IAM hydrolase activity were isolated. The results suggest the possibility that the activity of IAM hydrolase is suppressed in free-living state in Rhizobium leguminosarum biovar viciae K5. In addition we detected the peak at the same t_R Of IAM by HPLC analysis using two columns when a large amount of L-tryptophan was added to the suspension of 5-methyltryptophan-resistant variants. Whether or not tryptophan-2-monooxygenase activity, however, actually works in Rhizobium cells remained to be solved.
- 日本植物生理学会の論文
著者
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SEKINE Masami
Department of Bioproduction Science, Faculty of Bioresources and Environmental Sciences, Ishikawa Pr
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Syono Kunihiko
Department Of Life Science Graduate School Of Arts And Sciences University Of Tokyo:(present Address
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Sekine Masami
Department Of Fermentation Technology Faculty Of Engineering Osaka University
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Kawaguchi M
Univ. Tokyo Tokyo Jpn
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Kawaguchi Masayoshi
Department Of Biological Sciences Graduate School Of Science The University Of Tokyo
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Syono Kunihiko
Department Of Pure And Applied Sciences College Of Arts And Sciences The University Of Tokyo
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Sekine Masami
Department Of Bioproduction Science Ishikawa Prefectural University
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