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Literature summary for 1.14.99.55 extracted from

  • Lo Leggio, L.; Simmons, T.J.; Poulsen, J.C.; Frandsen, K.E.; Hemsworth, G.R.; Stringer, M.A.; von Freiesleben, P.; Tovborg, M.; Johansen, K.S.; De Maria, L.; Harris, P.V.; Soong, C.L.; Dupree, P.; Tryfona, T.; Lenfant, N.; Henrissat, B.; Davies, G.J.; Walton, P.H.
    Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase (2015), Nat. Commun., 6, 5961.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Aspergillus nidulans

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling of structure Aspergillus nidulans

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ Kd value 26 nM, protein shows a mononuclear copper-based EPR signal Aspergillus nidulans

Organism

Organism UniProt Comment Textmining
Aspergillus nidulans
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no oxidative activity with phosphoric acid-swollen cellulose, chitin, polygalacturonan or esterified pectin Aspergillus nidulans ?
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?
starch + cysteine + O2
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Aspergillus nidulans malto-oligosaccharide aldonic acid + cystine + H2O C1-oxidized maltooligosaccharides with a degree of polymerization from DP5 to DP13, unmodified oligosaccharide species are not observed ?

Synonyms

Synonyms Comment Organism
AA13 CAZY auxilliary activity family 13 Aspergillus nidulans

General Information

General Information Comment Organism
physiological function enzyme acts in synergy with glycoside hydrolase, beta-amylase, largely enhancing maltose release from retrograded starch by beta-amylase. The largest enhancements are obtained under specific conditions using the reducing cofactor cysteine, the presence of LPMO enhances the release of maltose by beta-amylase by 100fold Aspergillus nidulans