Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 20, Issue 18, Pages -Publisher
MDPI
DOI: 10.3390/ijms20184594
Keywords
lytic polysaccharide monooxygenases; LPMOs; substrate specificity; regioselectivity
Funding
- Guangdong Province Science and Technology Innovation Strategy Special Fund [2018B020205001]
- GDAS' Special Project of Science and Technology Development [2018GDASCX-0908]
- Science and Technology Plan Project of Guangdong Province [2015A020211022, 2019B030316017]
- National Natural Science Foundation of China [31400681]
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Lytic polysaccharide monooxygenases (LPMOs) are key enzymes in both the natural carbon cycle and the biorefinery industry. Understanding the molecular basis of LPMOs acting on polysaccharide substrates is helpful for improving industrial cellulase cocktails. Here we analyzed the sequences, structures, and substrate binding modes of LPMOs to uncover the factors that influence substrate specificity and regioselectivity. Our results showed that the different compositions of a motif located on L2 affect the electrostatic potentials of substrate binding surfaces, which in turn affect substrate specificities of AA10 LPMOs. A conserved Asn at a distance of 7 angstrom from the active center Cu might, together with the conserved Ser immediately before the second catalytic His, determine the localization of LPMOs on substrate, and thus contribute to C4-oxidizing regioselectivity. The findings in this work provide an insight into the molecular basis of substrate specificity and regioselectivity of LPMOs.
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