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- Description of Luteibacter aegosomatis sp. nov., Luteibacter aegosomaticola sp. nov., and Luteibacter aegosomatissinici sp. nov. isolated from the Intestines of Aegosoma sinicum Larvae
- Hae-In Joe , Jee-Won Choi , June-Young Lee , Hojun Sung , Su-Won Jeong , Yun-Seok Jeong , Jae-Yun Lee , Jin-Woo Bae
- J. Microbiol. 2023;61(6):603-613. Published online May 5, 2023
- DOI: https://doi.org/10.1007/s12275-023-00051-7
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Abstract
- Three novel bacterial strains, 321T, 335T, and 353T, were isolated from the intestines of Aegosoma sinicum larvae collected from Paju-Si, South Korea. The strains were Gram-negative, obligate aerobe and had rod-shaped cells with a single flagellum. The three strains belonged to the genus Luteibacter in the family Rhodanobacteraceae and shared < 99.2% similarity in their 16S rRNA gene sequence and < 83.56% similarity in thier whole genome sequence. Strains 321T, 335T, and 353T formed a monophyletic clade with Luteibacter yeojuensis KACC 11405T, L. anthropi KACC 17855T, and L. rhizovicinus KACC 12830T, with sequence similarities of 98.77–98.91%, 98.44–98.58%, and 97.88–98.02%, respectively. Further genomic analyses, including the construction of the Up-to-date Bacterial Core Gene (UBCG) tree and assessment of other genome-related indices, indicated that these strains were novel species belonging to the genus Luteibacter. All three strains contained ubiquinone Q8 as their major isoprenoid quinone and iso-C15:0 and summed feature 9 ( C16:0 10-methyl and/or iso-C17:1 ω9c) as their major cellular fatty acids. Phosphatidylethanolamine and diphosphatidylglycerol were the major polar lipids in all the strains. The genomic DNA G + C contents of strains 321T, 335T, and 353T were 66.0, 64.5, and 64.5 mol%, respectively. Based on multiphasic classification, strains 321T, 335T, and 353T were classified into the genus Luteibacter as the type strains of novel species, for which the names Luteibacter aegosomatis sp. nov., Luteibacter aegosomaticola sp. nov., and Luteibacter aegosomatissinici sp. nov. are proposed, respectively.
- Role of the Amino Acid Residued in the Catalysis of Catechol 2,3-dioxygenase from Pseudomonas putida SU10 as Probed by Chemical Modification and Random Mutagenesis
- Park, Sun Jung , park, Jin Mo , Lee, Byeong Jae , Min, Kyung Hee
- J. Microbiol. 1997;35(4):300-308.
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Abstract
- The catechol 2,3-dioxygenase (C23O) encoded by the Pseudomonas putida xylE gene was over-produced in Escherichia coli and purified to homogeneity. The activity of the C23O required the reduced form of the Fe(II) ion since the enzyme was highly susceptible to inactivation with hydrogen perocide but reactivated with the addition of ferrous sulfate in conjunction with ascorbic acid. The C23O activity was abolished by treatment with the chemical reagents, diethyl-pyrocarbonate (DEPC), tetranitromethane (TNM), and 1-cyclohexy1-3-(2-morpholinoethyl) car-bodiimidemetho-ρ-toluenesulfontate (CMC), which are modifying reagents of histidine, tyrosine and glutamic acid, respectively. These results suggest that histidine, tyrosine and glutamic acid residues may be good active sites for the enzyme activity. These amino acid residues are conserved residues may be good active sites for the enzyme activity. These amino acid residues are conserved residues among several extradion dioxygenases and have the chemical potential to serveas ligands for Fe(II) coordination. Analysis of random point mutants in the C23O gene derived by PCR technique revealed that the mutated positions of two mutants, T179S and S211R, were located near the conserved His165 amd Hos217 residues, respectively. This finding indicates that these two positions, along with the conserved histidine residues, are specially effective regions for the enzyme function.
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