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Literature summary for 1.14.99.56 extracted from

  • Vermaas, J.V.; Crowley, M.F.; Beckham, G.T.; Payne, C.M.
    Effects of lytic polysaccharide monooxygenase oxidation on cellulose structure and binding of oxidized cellulose oligomers to cellulases (2015), J. Phys. Chem. B, 119, 6129-6143.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
cellobiose little product inhibition Trichoderma reesei

Organism

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

General Information

General Information Comment Organism
physiological function the enzyme prefers oxidation of products at C4, which lowers product binding affinity and thereby should enhance product release and processive hydrolytic turnover. Product inhibition resulting from binding of oxidized products is likely not significant Trichoderma reesei