The Enzyme Database

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Accepted name: lytic cellulose monooxygenase (C4-dehydrogenating)
Reaction: [(1→4)-β-D-glucosyl]n+m + reduced acceptor + O2 = 4-dehydro-β-D-glucosyl-[(1→4)-β-D-glucosyl]n-1 + [(1→4)-β-D-glucosyl]m + acceptor + H2O
Systematic name: cellulose, hydrogen-donor:oxygen oxidoreductase (D-glucosyl 4-dehydrogenating)
Comments: This copper-containing enzyme, found in fungi and bacteria, cleaves cellulose in an oxidative manner. The cellulose fragments that are formed contain a 4-dehydro-D-glucose residue at the non-reducing end. Some enzymes also oxidize cellulose at the C-1 position of the reducing end forming a D-glucono-1,5-lactone residue [cf. EC, lytic cellulose monooxygenase (C1-hydroxylating)].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Beeson, W.T., Phillips, C.M., Cate, J.H. and Marletta, M.A. Oxidative cleavage of cellulose by fungal copper-dependent polysaccharide monooxygenases. J. Am. Chem. Soc. 134 (2012) 890–892. [DOI] [PMID: 22188218]
2.  Li, X., Beeson, W.T., 4th, Phillips, C.M., Marletta, M.A. and Cate, J.H. Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases. Structure 20 (2012) 1051–1061. [DOI] [PMID: 22578542]
3.  Forsberg, Z., Mackenzie, A.K., Sorlie, M., Rohr, A.K., Helland, R., Arvai, A.S., Vaaje-Kolstad, G. and Eijsink, V.G. Structural and functional characterization of a conserved pair of bacterial cellulose-oxidizing lytic polysaccharide monooxygenases. Proc. Natl. Acad. Sci. USA 111 (2014) 8446–8451. [DOI] [PMID: 24912171]
4.  Borisova, A.S., Isaksen, T., Dimarogona, M., Kognole, A.A., Mathiesen, G., Varnai, A., Rohr, A.K., Payne, C.M., Sorlie, M., Sandgren, M. and Eijsink, V.G. Structural and functional characterization of a lytic polysaccharide monooxygenase with broad substrate specificity. J. Biol. Chem. 290 (2015) 22955–22969. [DOI] [PMID: 26178376]
5.  Patel, I., Kracher, D., Ma, S., Garajova, S., Haon, M., Faulds, C.B., Berrin, J.G., Ludwig, R. and Record, E. Salt-responsive lytic polysaccharide monooxygenases from the mangrove fungus Pestalotiopsis sp. NCi6. Biotechnol Biofuels 9:108 (2016). [DOI] [PMID: 27213015]
[EC created 2017]

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