EC Number   |
|---|
  1.5.3.25 | homology modeling and docking of substrates fructosyl L-valine and Nepsilon-fructosyl-L-lysine. Residue Asn354 interacts closely with Nepsilon-fructosyl-L-lysine, but not with fructosyl L-valine |
| 1.5.3.25 | homology modeling of structure. Asn354 plays an important role in substrate recognition and can be substituted in order to change substrate specificity while maintaining high catalytic activity |
| 1.5.3.25 | mutant T60A/A188G/M244L/N257S/L261M, giving rhombic prismatic yellow crystals, space group C2 with unit-cell parameters a 101.08, b 63.36, c 83.07 A, beta 108.8°, to at least 1.8 A resolution, and additionally rod-like crystals, space group P4122 or P4322 with unitcell parameters a = b = 119.09, c 164.66 A and diffract to 2.7 A resolution |
| 1.5.3.25 | structure of FAOX-II shows an interaction between Lys53 and the isoalloxazine. The ammonium nitrogen of the lysine is in contact with and nearly centered over the aromatic ring of the flavin on the si-face. The positive charge of Lys53 is critical for flavin reduction, but plays very little role in the reaction with molecular oxygen |
| 1.5.3.25 | structures in free form and in complex with the inhibitor fructosyl-thioacetate, at 1.75 and 1.6 A resolution, respectively. FAOX-II is a two domain FAD-enzyme with an overall topology similar to that of monomeric sarcosine oxidase. Active site residues Tyr-60, Arg-112 and Lys-368 bind the carboxylic portion of the fructosamine, whereas Glu-280 and Arg-411 bind the fructosyl portion |
| 1.5.3.25 | structures of the free and the substrate-bound form of amadoriase I and comparison with isoform amadoriase II. While in Amadoriase II the loop 59-70 (amadoriase I numbering) is directed toward the core of the protein, in amadoriase I the loop is projected outward and is exposed to the solvent, contributing to the formation of a larger catalytic cavity |
