Literature summary for 1.1.3.7 extracted from

Carro, J.; Martinez-Julvez, M.; Medina, M.; Martinez, A.T.; Ferreira, P.
Protein dynamics promote hydride tunnelling in substrate oxidation by aryl-alcohol oxidase (2017), Phys. Chem. Chem. Phys., 19, 28666-28675 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure in complex with 4-anisidic acid	Pleurotus eryngii

Protein Variants

Protein Variants	Comment	Organism
Y92F	mutation of active site, residue is involved in modulating the hydride transfer reaction	Pleurotus eryngii
Y92L	mutation of active site, residue is involved in modulating the hydride transfer reaction	Pleurotus eryngii
Y92W	mutation of active site, residue is involved in modulating the hydride transfer reaction	Pleurotus eryngii

Organism

Organism	UniProt	Comment	Textmining
Pleurotus eryngii	O94219	-	-

General Information

General Information	Comment	Organism
metabolism	temperature dependence of hydride transfer from the substrate to the N5 of the FAD cofactor during the reductive half-reaction. Kinetic isotope effects suggest an environmentally-coupled quantum-mechanical tunnelling process. AAO shows a preorganized active site that would only require the approaching of the hydride donor and acceptor for the tunnelled transfer to take place	Pleurotus eryngii

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Release 2023.1 (January 2023)