8XAC
Crystal structure of amidase from Pseudonocardia acaciae
Summary for 8XAC
| Entry DOI | 10.2210/pdb8xac/pdb |
| Descriptor | Amidase family protein (2 entities in total) |
| Functional Keywords | amidase, hydrolase |
| Biological source | Pseudonocardia acaciae |
| Total number of polymer chains | 4 |
| Total formula weight | 198544.39 |
| Authors | |
| Primary citation | Takenoya, M.,Hiratsuka, Y.,Shimamura, K.,Ito, S.,Sasaki, Y.,Yajima, S. Characterizing an amidase and its operon from actinomycete bacteria responsible for paraben catabolism. Biosci.Biotechnol.Biochem., 88:1047-1054, 2024 Cited by PubMed 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. PubMed: 38886122DOI: 10.1093/bbb/zbae083 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.02 Å) |
Structure validation
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