Literature summary for 1.14.99.54 extracted from

Hansson, H.; Karkehabadi, S.; Mikkelsen, N.; Douglas, N.; Kim, S.; Lam, A.; Kaper, T.; Kelemen, B.; Meier, K.; Jones, S.; Solomon, E.; Sandgren, M.
High-resolution structure of a lytic polysaccharide monooxygenase from Hypocrea jecorina reveals a predicted linker as an integral part of the catalytic domain (2017), J. Biol. Chem., 292, 19099-19109 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Hypocrea jecorina	Trichoderma reesei

Crystallization (Commentary)

Crystallization (Comment)	Organism
C-terminally truncated variant containing 21 residues of the predicted linker domain, to 0.95 A resolution. The linker forms an integral part of the catalytic domain structure, covering a hydrophobic patch on the catalytic AA9 module. The oxidized catalytic center contains a Cu(II) coordinated by two His ligands, one of which has a His-brace in which the His-1 terminal amine group also coordinates to a copper. The final equatorial position of the Cu(II) is occupied by a water-derived ligand	Trichoderma reesei

Crystallization (Comment)

Organism

C-terminally truncated variant containing 21 residues of the predicted linker domain, to 0.95 A resolution. The linker forms an integral part of the catalytic domain structure, covering a hydrophobic patch on the catalytic AA9 module. The oxidized catalytic center contains a Cu(II) coordinated by two His ligands, one of which has a His-brace in which the His-1 terminal amine group also coordinates to a copper. The final equatorial position of the Cu(II) is occupied by a water-derived ligand

Trichoderma reesei

Protein Variants

Protein Variants	Comment	Organism
additional information	construction of a C-terminally truncated variant containing 21 residues of the predicted linker domain. The truncated variant exhibits reduced binding to cellulose and about 50% of wild-type activity on cellulose	Trichoderma reesei

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cu2+	the oxidized catalytic center contains a Cu(II) coordinated by two His ligands, one of which has a His-brace in which the His-1 terminal amine group also coordinates to a copper. The final equatorial position of the Cu(II) is occupied by a water-derived ligand	Trichoderma reesei

Organism

Organism	UniProt	Comment	Textmining
Trichoderma reesei	G0R6T8	-	-
Trichoderma reesei QM6a	G0R6T8	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
phosphoric acid swollen cellulose + ascorbic acid + O2	-	Trichoderma reesei	? + dehydroascorbic acid + H2O	-	?
phosphoric acid swollen cellulose + ascorbic acid + O2	-	Trichoderma reesei QM6a	? + dehydroascorbic acid + H2O	-	?

Synonyms

Synonyms	Comment	Organism
LPMO9A	-	Trichoderma reesei