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EC Number	Substrates	Commentary Substrates	Products	Commentary (Products)	Reversibility
1.14.99.53	[(1->4)-N-acetyl-beta-D-glucosaminyl]n+m + reduced acceptor + O2	-	[(1->4)-N-acetyl-beta-D-glucosaminyl]m-1-(1->4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O	-	?
1.14.99.53	[(1->4)-N-acetyl-beta-D-glucosaminyl]6 + ascorbate + O2	-	[(1->4)-N-acetyl-beta-D-glucosaminyl]3-(1->4)-N-acetyl-2-deoxy-2-amino-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]2 + dehydroascorbate + H2O	-	?
1.14.99.53	phosphoric acid swollen cellulose + ascorbate + O2	reaction of EC 1.14.99.54	C4-oxidized cellooligosaccharides + C1/C4-oxidized cellooligosaccharides + dehydroascorbate + H2O	-	?
1.14.99.53	phosphoric acid swollen cellulase + ascorbic acid + O2	-	? + dehydroascorbate + H2O	-	?
1.14.99.53	more	data indicate that catalysis involves equatorial binding of a reactive oxygen species	?	-	?
1.14.99.53	more	the enzyme produces oxidized chitin oligosaccharides with a degree of polymerization from DPox3 to DPox11. The relative intensities of DPox4, DPox6, DPox8 and DPox10 are remarkably higher than DPox5, DPox7, DPox9 and DPox11. LPMO10A shows little binding to Avicel	?	-	?
1.14.99.53	more	no activity on other substrates including diverse mannans, cellulose and starch	?	-	?
1.14.99.53	more	enzyme in presence of ascorbate but lacking chitin produces H2O2	?	-	?
1.14.99.53	more	mechanistic model, copper is reduced on the enzyme by an externally provided electron and followed by oxygen binding and activation by internal electron transfer. Substrate binding involves an extended planar binding surface, including the metal binding site. Chitin binding protects two regions from 2H/1H exchange, Gln53-Ser58 and Leu110-Thr116	?	-	?
1.14.99.53	more	isoform LPMO10B produces C4-oxidized (4-ketoaldoses) and double (C4/C1)-oxidized cello-oligosaccharides. No substrate: alpha-chitin	?	-	?

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