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Literature summary for 1.5.3.25 extracted from

  • Collard, F.; Fagan, R.; Zhang, J.; Nemet, I.; Palfey, B.; Monnier, V.
    The cation-pi interaction between Lys53 and the flavin of fructosamine oxidase (FAOX-II) is critical for activity (2011), Biochemistry, 50, 7977-7986 .
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

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

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

Inhibitors Comment Organism Structure
fructosyl-thioacetate Kd value 3.4 microM Aspergillus fumigatus

Organism

Organism UniProt Comment Textmining
Aspergillus fumigatus P78573
-
-

Cofactor

Cofactor Comment Organism Structure
FAD covalently bound Aspergillus fumigatus

General Information

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