8xac | pdb_00008xac

Crystal structure of amidase from Pseudonocardia acaciae

spinqualitylabelsall models 8xac, resolution 3.02Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8xac is a 4 chain structure with sequence from Pseudonocardia acaciae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.02Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. Characterizing an amidase and its operon from actinomycete bacteria responsible for paraben catabolism.,Takenoya M, Hiratsuka Y, Shimamura K, Ito S, Sasaki Y, Yajima S Biosci Biotechnol Biochem. 2024 Aug 26;88(9):1047-1054. doi: 10.1093/bbb/zbae083. PMID:38886122 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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