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Literature summary for 1.14.99.54 extracted from

  • Eibinger, M.; Sattelkow, J.; Ganner, T.; Plank, H.; Nidetzky, B.
    Single-molecule study of oxidative enzymatic deconstruction of cellulose (2017), Nat. Commun., 8, 894 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
single-molecule study by atomic force microscopy Neurospora crassa

Organism

Organism UniProt Comment Textmining
Neurospora crassa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cellulose + reduced acceptor + O2
-
Neurospora crassa ? + oxidized acceptor + H2O
-
?

Synonyms

Synonyms Comment Organism
LPMO9C
-
Neurospora crassa
LPMO9f
-
Neurospora crassa

General Information

General Information Comment Organism
physiological function isoforms LPMO9C and LPMO9F bind to nanocrystalline cellulose with high preference for the very same substrate surfaces that are also used by Hypocrea jecorina processive cellulase CBH I to move along during hydrolytic cellulose degradation. The bound LPMOs are immobile during their adsorbed residence time on cellulose. Treatment with LPMO results in fibrillation of crystalline cellulose, enhances the cellulase adsorption more than 2fold and increases enzyme turnover on the cellulose surface, boosting the hydrolytic conversion Neurospora crassa