5OC1

Crystal structure of aryl-alcohol oxidase from Pleurotus eryngii in complex with p-anisic acid

Summary for 5OC1

• Entry DOI: 10.2210/pdb5oc1/pdb
• Descriptor: Aryl-alcohol oxidase, 4-METHOXYBENZOIC ACID, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: aao, lignin degradation, pleurotus eryngii, oxidoreductase, flavoprotein
• Biological source: Pleurotus eryngii
• Total number of polymer chains: 1
• Total formula weight: 62329.70

Authors

Carro, J.,Martinez-Julvez, M.,Medina, M.,Martinez, A.,Ferreira, P. (deposition date: 2017-06-29, release date: 2017-11-01, Last modification date: 2024-01-17)

Primary citation

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

PubMed Abstract: The temperature dependence of hydride transfer from the substrate to the N5 of the FAD cofactor during the reductive half-reaction of Pleurotus eryngii aryl-alcohol oxidase (AAO) is assessed here. Kinetic isotope effects on both the pre-steady state reduction of the enzyme and its steady-state kinetics, with differently deuterated substrates, suggest an environmentally-coupled quantum-mechanical tunnelling process. Moreover, those kinetic data, along with the crystallographic structure of the enzyme in complex with a substrate analogue, indicate that AAO shows a pre-organized active site that would only require the approaching of the hydride donor and acceptor for the tunnelled transfer to take place. Modification of the enzyme's active-site architecture by replacement of Tyr92, a residue establishing hydrophobic interactions with the substrate analogue in the crystal structure, in the Y92F, Y92L and Y92W variants resulted in different temperature dependence patterns that indicated a role of this residue in modulating the transfer reaction.

PubMed: 29043303
DOI: 10.1039/c7cp05904c

Experimental method

X-RAY DIFFRACTION (2.3 Å)