TY  - JOUR
A1  - Coelho, Catarina
A1  - Mahro, Martin
A1  - Trincao, Jose
A1  - Carvalho, Alexandra T. P.
A1  - Ramos, Maria Joao
A1  - Terao, Mineko
A1  - Garattini, Enrico
A1  - Leimkühler, Silke
A1  - Romao, Maria Joao
T1  - The first mammalian aldehyde oxidase crystal structure insights into substrate specificity
JF  - The journal of biological chemistry
N2  - Aldehyde oxidases (AOXs) are homodimeric proteins belonging to the xanthine oxidase family of molybdenum-containing enzymes. Each 150-kDa monomer contains a FAD redox cofactor, two spectroscopically distinct [2Fe-2S] clusters, and a molybdenum cofactor located within the protein active site. AOXs are characterized by broad range substrate specificity, oxidizing different aldehydes and aromatic N-heterocycles. Despite increasing recognition of its role in the metabolism of drugs and xenobiotics, the physiological function of the protein is still largely unknown. We have crystallized and solved the crystal structure of mouse liver aldehyde oxidase 3 to 2.9 angstrom. This is the first mammalian AOX whose structure has been solved. The structure provides important insights into the protein active center and further evidence on the catalytic differences characterizing AOX and xanthine oxidoreductase. The mouse liver aldehyde oxidase 3 three-dimensional structure combined with kinetic, mutagenesis data, molecular docking, and molecular dynamics studies make a decisive contribution to understand the molecular basis of its rather broad substrate specificity.
Y1  - 2012
U6  - https://doi.org/10.1074/jbc.M112.390419
SN  - 0021-9258
VL  - 287
IS  - 48
SP  - 40690
EP  - 40702
PB  - American Society for Biochemistry and Molecular Biology
CY  - Bethesda
ER  -