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Literature summary for 2.7.7.2 extracted from

  • Arilla-Luna, S.; Serrano, A.; Medina, M.
    Specific features for the competent binding of substrates at the FMN adenylyltransferase site of FAD synthase from Corynebacterium ammoniagenes (2019), Int. J. Mol. Sci., 20, 5083 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
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 Corynebacterium ammoniagenes

Protein Variants

Protein Variants Comment Organism
L98A mutation totally prevents the binding of FMN and/or FAD. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis Corynebacterium ammoniagenes
L98K mutation totally prevents the binding of FMN and/or FAD. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis Corynebacterium ammoniagenes
L98W residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis Corynebacterium ammoniagenes
P56A/P58A variant exhibits lower KdATP values and altered thermodynamic profile for ATP binding. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis Corynebacterium ammoniagenes
P56W variant exhibits lower KdATP values and altered thermodynamic profile for ATP binding. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis Corynebacterium ammoniagenes
P58W residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis Corynebacterium ammoniagenes

Organism

Organism UniProt Comment Textmining
Corynebacterium ammoniagenes Q59263
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + FMN
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 Corynebacterium ammoniagenes diphosphate + FAD
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