AI Article Synopsis
- Polyacrylamide (PAM) is a durable polymer that doesn’t break down easily, leading to environmental issues due to its accumulation.
- A study identified two key enzymes (amidohydrolases) in Klebsiella sp. PCX that effectively degrade PAM, outperforming many smaller compounds.
- The researchers also determined the structures of these enzymes and pinpointed specific active sites that facilitate their function, which can aid in future PAM bioremediation efforts.
Article Abstract
Polyacrylamide (PAM) is a high molecular weight polymer with extensive applications. However, inefficient natural degradation of PAM results in its environmental accumulation. Here, using multi-omics analysis, we constructed the PAM biodegradation pathway in Klebsiella sp. PCX, an efficient PAM-degrading bacterium. Subsequently, two unclassified amidohydrolases (PCX00451 and PCX04581) were identified as key factors for rapid PAM biodegradation, both of which possessed much higher hydrolysis efficiency for PAM than for small molecule amide compounds. Besides, crystal structures of PCX00451 and PCX04581 were solved. Both two amidohydrolases were consisted with a twisted triosephosphateisomerase (TIM)-barrel and a smaller β-sandwich domain. And their binding pockets were in the conserved metal center of TIM-barrel domain. Moreover, Asp267 of PCX00451 and Asp282 of PCX04581 were examined as active sites for acid/base catalysis. Our research characterized the molecular mechanisms of two efficient amidohydrolases, providing theoretical basis and valuable tools for PAM bioremediation.
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| http://dx.doi.org/10.1016/j.ijbiomac.2024.136329 | DOI Listing |
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