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Literature summary extracted from

  • Frago, S.; Martinez-Julvez, M.; Serrano, A.; Medina, M.
    Structural analysis of FAD synthetase from Corynebacterium ammoniagenes (2008), BMC Microbiol., 8, 160.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.2 expression in Escherichia coli Corynebacterium ammoniagenes

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.2 3D structural model for based on the structure of Thermotoga maritima FADS Corynebacterium ammoniagenes

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.2 E268A active, involved in riboflavin kinase activity Corynebacterium ammoniagenes
2.7.7.2 E268D active, involved in riboflavin kinase activity Corynebacterium ammoniagenes
2.7.7.2 H28A loss of both riboflavin kinase and FAD synthetase activities Corynebacterium ammoniagenes
2.7.7.2 H28D loss of both riboflavin kinase and FAD synthetase activities Corynebacterium ammoniagenes
2.7.7.2 H31D residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN Corynebacterium ammoniagenes
2.7.7.2 N210A active, involved in riboflavin kinase activity Corynebacterium ammoniagenes
2.7.7.2 N210D active, involved in riboflavin kinase activity Corynebacterium ammoniagenes
2.7.7.2 R161A active, residue R161 does not play a critical role in catalysis Corynebacterium ammoniagenes
2.7.7.2 R161D active, residue R161 does not play a critical role in catalysis Corynebacterium ammoniagenes
2.7.7.2 S164A residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN Corynebacterium ammoniagenes
2.7.7.2 S164D residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN Corynebacterium ammoniagenes
2.7.7.2 T165A residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN Corynebacterium ammoniagenes
2.7.7.2 T165D residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN Corynebacterium ammoniagenes
2.7.7.2 T208A active, involved in riboflavin kinase activity Corynebacterium ammoniagenes
2.7.7.2 T208D active, involved in riboflavin kinase activity Corynebacterium ammoniagenes

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.2 Corynebacterium ammoniagenes Q59263 bifunctional enzyme, displays activities of EC 2.7.7.2 and EC 2.7.1.26
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Cofactor

EC Number Cofactor Comment Organism Structure
2.7.7.2 flavin presence of a flavin binding site for the adenylylation activity, independent from that related with the phosphorylation actiity Corynebacterium ammoniagenes