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

Authors :
Takenoya M
Hiratsuka Y
Shimamura K
Ito S
Sasaki Y
Yajima S
Source :
Bioscience, biotechnology, and biochemistry [Biosci Biotechnol Biochem] 2024 Aug 26; Vol. 88 (9), pp. 1047-1054.
Publication Year :
2024

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.<br /> (© The Author(s) 2024. Published by Oxford University Press on behalf of Japan Society for Bioscience, Biotechnology, and Agrochemistry.)

Details

Language :
English
ISSN :
1347-6947
Volume :
88
Issue :
9
Database :
MEDLINE
Journal :
Bioscience, biotechnology, and biochemistry
Publication Type :
Academic Journal
Accession number :
38886122
Full Text :
https://doi.org/10.1093/bbb/zbae083