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@article{586887,
author = {Sato, Yukari and Monincová, Marta and Chaloupková, Radka and Prokop, Zbyněk and Ohtsubo, Yoshiyuki and Minamisawa, Kiwamu and Tsuda, Masataka and Damborský, Jiří and Nagata, Yuji},
article_number = {8},
keywords = {Haloalkane dehalogenases;rhizobial strains;Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110;},
language = {eng},
issn = {0099-2240},
journal = {APPLIED AND ENVIRONMENTAL MICROBIOLOGY},
title = {Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities},
url = {http://loschmidt.chemi.muni.cz/peg/pdf/aem05b.pdf},
volume = {71},
year = {2005}
}
TY - JOUR
ID - 586887
AU - Sato, Yukari - Monincová, Marta - Chaloupková, Radka - Prokop, Zbyněk - Ohtsubo, Yoshiyuki - Minamisawa, Kiwamu - Tsuda, Masataka - Damborský, Jiří - Nagata, Yuji
PY - 2005
TI - Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities
JF - APPLIED AND ENVIRONMENTAL MICROBIOLOGY
VL - 71
IS - 8
SP - 43724379
EP - 43724379
SN - 00992240
KW - Haloalkane dehalogenases;rhizobial strains;Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110;
UR - http://loschmidt.chemi.muni.cz/peg/pdf/aem05b.pdf
N2 - Haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants. Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, have open reading frames (ORFs), mlr5434 and blr1087, respectively, that encode putative haloalkane dehalogenase homologues. The crude extracts of Escherichia coli strains expressing mlr5434 and blr1087 showed the ability to dehalogenate 18 halogenated compounds, indicating that these ORFs indeed encode haloalkane dehalogenases. Therefore, these ORFs were referred to as dmlA (dehalogenase from Mesorhizobium loti) and dbjA (dehalogenase from Bradyrhizobium japonicum), respectively. The principal component analysis of the substrate specificities of various haloalkane dehalogenases clearly showed that DbjA and DmlA constitute a novel substrate specificity class with extraordinarily high activity towards beta-methylated compounds. Comparison of the circular dichroism spectra of DbjA and other dehalogenases strongly suggested that DbjA contains more alpha-helices than the other dehalogenases. The dehalogenase activity of resting cells and Northern blot analyses both revealed that the dmlA and dbjA genes were expressed under normal culture conditions in MAFF303099 and USDA110 stain cells, respectively.
ER -
SATO, Yukari, Marta MONINCOVÁ, Radka CHALOUPKOVÁ, Zbyněk PROKOP, Yoshiyuki OHTSUBO, Kiwamu MINAMISAWA, Masataka TSUDA, Jiří DAMBORSKÝ a Yuji NAGATA. Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities. \textit{APPLIED AND ENVIRONMENTAL MICROBIOLOGY}. 2005, roč.~71, č.~8, s.~43724379-43724386. ISSN~0099-2240.
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