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Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Environmental Science / Faculty of Environmental Earth Science >
Peer-reviewed Journal Articles, etc >
Gentisate 1,2-dioxygenase from Xanthobacter polyaromaticivorans 127W.
| Title: | Gentisate 1,2-dioxygenase from Xanthobacter polyaromaticivorans 127W. |
| Authors: | Hirano, Shin-ichi Browse this author | | Morikawa, Masaaki Browse this author →KAKEN DB | | Takano, Kazufumi Browse this author | | Imanaka, Tadayuki Browse this author | | Kanaya, Shigenori Browse this author |
| Keywords: | gentisate 1,2-dioxygenase | | Xanthobacter | | gentisate | | naphthoate | | ferric ion |
| Issue Date: | Jan-2007 |
| Publisher: | Japan Society for Bioscience, Biotechnology, and Agrochemistry |
| Journal Title: | Bioscience, Biotechnology, and Biochemistry |
| Volume: | 71 |
| Issue: | 1 |
| Start Page: | 192 |
| End Page: | 199 |
| Publisher DOI: | 10.1271/bbb.60444 |
| PMID: | 17213679 |
| Abstract: | 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. |
| Relation: | http://www.jstage.jst.go.jp/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/29919 |
| Appears in Collections: | 環境科学院・地球環境科学研究院 (Graduate School of Environmental Science / Faculty of Environmental Earth Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 森川 正章
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