Abstract
Lytic polysaccharide monooxygenases (LPMOs) are redox enzymes targeting the crystalline region of recalcitrant polysaccharides such as cellulose and chitin. Functional characterization of two LPMOs from the cellulose-degrading soil bacterium Cellulomonas gelida, CgLPMO10A and CgLPMO10B, showed expected activities on cellulose but also revealed novel features of AA10 LPMOs. While clustering together with strictly C1-oxidizing and strictly cellulose-active AA10 LPMOs, CgLPMO10A exhibits activity on both cellulose and chitin, oxidizing the C1 carbon of both substrates. This combination of substrate and oxidative specificity has not been previously observed for family 10 LPMOs and may be due to a conspicuous divergence in two hydrophobic residues on the substrate-binding surface. CgLPMO10B oxidizes cellulose at both the C1 and C4 positions and is also active on chitin, in line with predictions based on phylogeny. Interestingly, while coming from the same organism and both acting on cellulose, the two enzymes have markedly different redox properties with CgLPMO10B displaying the lowest redox potential and the highest oxidase activity observed for an AA10 LPMO so far. These results provide insight into the LPMO machinery of C. gelida and expand the known catalytic repertoire of bacterial LPMOs.