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Literature summary for 1.14.99.54 extracted from

  • Kim, S.; Stahlberg, J.; Sandgren, M.; Paton, R.S.; Beckham, G.T.
    Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism (2014), Proc. Natl. Acad. Sci. USA, 111, 149-154.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ the active catalyst is Cu(II)-oxyl Thermoascus aurantiacus

Organism

Organism UniProt Comment Textmining
Thermoascus aurantiacus G3XAP7
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cellulose + ascorbate + O2
-
Thermoascus aurantiacus ? + dehydroascorbate + H2O
-
?
additional information quantum mechanical calculations predict that oxygen binds end-on to copper, and that a copperoxyl-mediated, oxygen-rebound mechanism is energetically preferred. The N-terminal histidine methylation has only a minor effect on the LPMO active site structure or reactivity for the examined steps Thermoascus aurantiacus ?
-
?

Synonyms

Synonyms Comment Organism
Gh61 isozyme a
-
Thermoascus aurantiacus