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Characterizing an amidase and its operon from actinomycete bacteria responsible for paraben catabolism. | LitMetric

AI Article Synopsis

  • Researchers discovered that hydrazidase from Microbacterium hydrocarbonoxydans can break down synthetic hydrazide compounds, allowing the bacteria to thrive on them as their only carbon source, although natural substrates weren't known until this study.
  • Kinetic tests showed that parabens can serve as substrates for hydrazidase, and when exposed to methylparaben, the bacteria expressed genes related to hydrazidase and an ABC transporter, enabling growth on this compound alone.
  • A search for similar enzymes revealed that other actinomycetes also have hydrazidase homologs, and further analysis indicated that an amidase from Pseudonocardia acaciae has structural and functional similarities to hydrazidase,

Article Abstract

Hydrazidase from Microbacterium hydrocarbonoxydans was revealed to catalyze synthetic hydrazide compounds, enabling the bacteria to grow with them as a 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 a sole carbon source was able to grow the bacteria. Furthermore, homology search was carried out revealing that several actinomycetes possess hydrazidase homologs 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 code the homologous operon, the enzymes with those operons may play a physiologically important role for bacterial survival with use of parabens.

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Source
http://dx.doi.org/10.1093/bbb/zbae083DOI Listing

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