Crystallization (Comment) | Organism |
---|---|
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 | Aspergillus fumigatus |
Protein Variants | Comment | Organism |
---|---|---|
K53M | more than a million-fold decrease in flavin reduction, while only slowing the oxygen reaction by about 30fold | Aspergillus fumigatus |
K53R | mutation has minor effects on catalysis | Aspergillus fumigatus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
fructosyl-thioacetate | Kd value 3.4 microM | Aspergillus fumigatus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus fumigatus | P78573 | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | covalently bound | Aspergillus fumigatus |
General Information | Comment | Organism |
---|---|---|
metabolism | the positive charge of Lys53 is very important for FAOX. Removal of the positive charge renders the enzyme practically dead with respect to flavin reduction. It is only the charge and not its distribution that is important | Aspergillus fumigatus |