Gentisate 1,2-dioxygenase from Xanthobacter polyaromaticivorans 127W.
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概要
- 論文の詳細を見る
A putative gentisate 1,2-dioxygenase was encoded in the dibenzothiophene degradation gene cluster (dbd) from Xanthobacter polyaromaticivorans 127W. The deduced amino acid sequence showed high sequence similarity with gentisate dioxygenases from Pseudomonas alcaligenes (AAD49427, 65% identical), Bradyrhizobium japonicum (NP_766750, 64%), and P. aeruginosa (ZP_00135722, 54%), and moderate similarity with 1-hydroxy-2-naphthoate dioxygenase from Nocardioides sp. KP7 (BAA31235, 33%) and salicylate dioxygenase from Pseudaminobacter salicylatoxidans (AAQ91293, 33%). The enzyme, GDOxp, was heterologously produced in Escherichia coli and purified to homogeneity. GDOxp formed a tetramer and exhibited high dioxygenase activity against 1,4-dihydroxy 2-naphthoate as well as gentisate, suggesting unusually broad substrate specificity. GDOxp easily released ferrous ion under unfavorable temperature and pH conditions to become an inactive monomer protein. An inactive monomer protein can reconstitute a tetramer structure and restore enzyme activity in a cooperative manner upon the addition of ferrous ion. Chymotryptic digestion and protein truncation experiments suggested that the N-terminal region is important for the tetramerization of GDOxp.
- Japan Society for Bioscience, Biotechnology, and Agrochemistryの論文
著者
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HIRANO Shin-ichi
Department of Applied Chemistry, Graduate School of Engineering, Nagoya University
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森川 正章
大阪大学大学院工学研究科物質・生命工学専攻:北海道大学大学院地球環境科学研究院環境生物科学部門
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TAKANO Kazufumi
Department of Material and Life Science, Osaka University
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KANAYA Shigenori
Department of Material and Life Science, Osaka University
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IMANAKA Tadayuki
Department of Synthetic and Biological Chemistry, Graduate School of Engineering, Kyoto University
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MORIKAWA MASAAKI
Department of Material and Life Scinece, Graduate Shool of Engineering, Osaka University
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Hirano Shin‐ichi
Division Of Nanomaterials Science Ecotopia Science Institute Nagoya University
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Hirano Shin-ichi
Central Research Laboratories Mercian Corp.
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