{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hall KR"],"funding":["European Research Council"],"pagination":["23040-23052"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11137697"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(21)"],"pubmed_abstract":["Lytic polysaccharide monooxygenases (LPMOs) catalyze the oxidative cleavage of glycosidic bonds in recalcitrant polysaccharides, such as cellulose and chitin, using a single copper cofactor bound in a conserved histidine brace with a more variable second coordination sphere. Cellulose-active LPMOs in the fungal AA9 family and in a subset of bacterial AA10 enzymes contain a His-Gln-Tyr second sphere motif, whereas other cellulose-active AA10s have an Arg-Glu-Phe motif. To shine a light on the impact of this variation, we generated single, double, and triple mutations changing the His<sup>216</sup>-Gln<sup>219</sup>-Tyr<sup>221</sup> motif in cellulose- and chitin-oxidizing <i>Ma</i>AA10B toward Arg-Glu-Phe. These mutations generally reduced enzyme performance due to rapid inactivation under"],"journal":["ACS omega"],"pubmed_title":["Impact of the Copper Second Coordination Sphere on Catalytic Performance and Substrate Specificity of a Bacterial Lytic Polysaccharide Monooxygenase."],"pmcid":["PMC11137697"],"funding_grant_id":["856446"],"pubmed_authors":["Schwaiger L","Ayuso-Fernandez I","Hall KR","Eijsink VGH","Ludwig R","Golten O","Mollatt M","Forsberg Z","Sorlie M"],"additional_accession":[]},"is_claimable":false,"name":"Impact of the Copper Second Coordination Sphere on Catalytic Performance and Substrate Specificity of a Bacterial Lytic Polysaccharide Monooxygenase.","description":"Lytic polysaccharide monooxygenases (LPMOs) catalyze the oxidative cleavage of glycosidic bonds in recalcitrant polysaccharides, such as cellulose and chitin, using a single copper cofactor bound in a conserved histidine brace with a more variable second coordination sphere. Cellulose-active LPMOs in the fungal AA9 family and in a subset of bacterial AA10 enzymes contain a His-Gln-Tyr second sphere motif, whereas other cellulose-active AA10s have an Arg-Glu-Phe motif. To shine a light on the impact of this variation, we generated single, double, and triple mutations changing the His<sup>216</sup>-Gln<sup>219</sup>-Tyr<sup>221</sup> motif in cellulose- and chitin-oxidizing <i>Ma</i>AA10B toward Arg-Glu-Phe. These mutations generally reduced enzyme performance due to rapid inactivation under","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-02T01:40:08.064Z","creation":"2026-04-13T03:12:47.154Z"},"accession":"S-EPMC11137697","cross_references":{"pubmed":["38826537"],"doi":["10.1021/acsomega.4c02666"]}}