AI Article Synopsis
- Laccases are important industrial enzymes, but their effectiveness is limited due to stability and functioning conditions, typically performing best in acidic environments and under 60 °C.
- Researchers studied a specific two-domain laccase (2D) from SgfSL that operates in alkaline conditions and elevated temperatures, identifying how polar residues near its trinuclear center (TNC) affect its activity.
- Mutations in the 2D laccase notably altered its activity and efficiency in oxidizing specific substrates, enhancing understanding of laccase structure and functioning, and paving the way for targeted enzyme engineering.
Article Abstract
Laccases are industrially relevant enzymes. However, their range of applications is limited by their functioning and stability. Most of the currently known laccases function in acidic conditions at temperatures below 60 °C, but two-domain laccases (2D) oxidize some substrates in alkaline conditions and above 70 °C. In this study, we aim to establish the structural factors affecting the alkaline activity of the 2D laccase from (SgfSL). The range of methods used allowed us to show that the alkaline activity of SgfSL is influenced by the polar residues located close to the trinuclear center (TNC). Structural and functional studies of the SgfSL mutants Met199Ala/Asp268Asn and Met199Gly/Asp268Asn revealed that the substitution Asp268Asn (11 Å from the TNC) affects the orientation of the Asn261 (the second coordination sphere of the TNC), resulting in hydrogen-bond-network reorganization, which leads to a change in the SgfSL-activity pH profile. The combination of the Met199Gly/Arg240His and Asp268Asn substitutions increased the efficiency (k/K) of the 2,6-DMP oxidation by 34-fold compared with the SgfSL. Our results extend the knowledge about the structure and functioning of 2D laccases' TNC active sites and open up new possibilities for the directed engineering of laccases.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10419308 | PMC |
| http://dx.doi.org/10.3390/ijms241511909 | DOI Listing |
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