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Literature summary for 2.7.7.2 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
Search for more literature for 2.7.7.2

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Corynebacterium ammoniagenes

Crystallization (Commentary)

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

Protein Variants

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

Organism

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

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