M. Takenoya, Yoshiaki Hiratsuka, K. Shimamura, Shinsaku Ito, Yasuyuki Sasaki, Shunsuke Yajima
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Characterizing an amidase and its operon from actinomycete bacteria responsible for paraben catabolism
Hydrazidase from Microbacterium hydrocarbonoxydans was revealed to catalyze synthetic hydrazide compounds, enabling the bacteria to grow with them as sole carbon source, but natural substrates have remained unknown.
In this study, kinetic analyses of hydrazidase with parabens showed that the compounds can be substrates. Then, methylparaben induced gene expressions of the operon containing hydrazidase and ABC transporter, and the compound as sole carbon source was able to grow the bacteria. Furthermore, homology search was carried out revealing that several actinomycetes possess hydrazidase-homolog in the operon. Among those bacteria, an amidase from Pseudonocardia acaciae was subjected to a kinetic analysis and a structure determination revealing similar but not identical to those of hydrazidase.
Since parabens are reported to exist in plants and soil, and several actinomycetes codes the homologous operon, the enzymes with those operons may play a physiologically important role for bacterial survival with use of parabens.
期刊介绍:
Bioscience, Biotechnology, and Biochemistry publishes high-quality papers providing chemical and biological analyses of vital phenomena exhibited by animals, plants, and microorganisms, the chemical structures and functions of their products, and related matters. The Journal plays a major role in communicating to a global audience outstanding basic and applied research in all fields subsumed by the Japan Society for Bioscience, Biotechnology, and Agrochemistry (JSBBA).