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Literature summary for 1.14.99.54 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

Organism

Organism UniProt Comment Textmining
Trichoderma reesei G0RVK1
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-
Trichoderma reesei QM6a G0RVK1
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-

Synonyms

Synonyms Comment Organism
Cel7A
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Trichoderma reesei

General Information

General Information Comment Organism
physiological function the enzyme produces both C1- and 4-oxidized products. The equilibrium between the two reducing end oxidized products, favoring the linear aldonic acid, may increase product inhibition, which would in turn reduce processive substrate turnover. In the case of action at the nonreducing end, oxidation appears to lower affinity with the nonreducing end specific cellulase, reducing product inhibition and potentially promoting processive cellulose turnover Trichoderma reesei