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Literature summary for 1.4.99.6 extracted from

  • Iyer, A.; Reis, R.A.G.; Gannavaram, S.; Momin, M.; Spring-Connell, A.M.; Orozco-Gonzalez, Y.; Agniswamy, J.; Hamelberg, D.; Weber, I.T.; Gozem, S.; Wang, S.; Germann, M.W.; Gadda, G.
    A single-point mutation in D-arginine dehydrogenase unlocks a transient conformational state resulting in altered cofactor reactivity (2021), Biochemistry, 60, 711-724 .
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
Y249F mutant protein shows both an active yellow FAD (Y249F-y) and an inactive chemically modified green 6-hydroxy-FAD cofactor. Variants show no differences in the overall protein structure and fold. Variant Y249F-y displays an alternative conformation for some active site residues and the flavin cofactor. Y249F-y with FAD samples a metastable conformational state, not available to the wild-type enzyme. The alternate conformation in the Y249F-y enzyme is responsible for the higher spin density at the C6 atom of flavin, consistent with the formation of 6-hydroxy-FAD Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa Q9HXE3
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Cofactor

Cofactor Comment Organism Structure
FAD mutant Y249F protein shows both an active yellow FAD (Y249F-y) and an inactive chemically modified green 6-hydroxy-FAD cofactor. Variants show no differences in the overall protein structure and fold. Variant Y249F-y displays an alternative conformation for some active site residues and the flavin cofactor. Y249F-y with FAD samples a metastable conformational state, not available to the wild-type enzyme. The alternate conformation in the Y249F-y enzyme is responsible for the higher spin density at the C6 atom of flavin, consistent with the formation of 6-hydroxy-FAD Pseudomonas aeruginosa