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Literature summary for 2.7.7.2 extracted from

  • Huerta, C.; Borek, D.; Machius, M.; Grishin, N.V.; Zhang, H.
    Structure and mechanism of a eukaryotic FMN adenylyltransferase (2009), J. Mol. Biol., 389, 388-400.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
His-tagged version expressed in Escherichia coli BL21(DE3) [Candida] glabrata

Crystallization (Commentary)

Crystallization (Comment) Organism
-
[Candida] glabrata

Protein Variants

Protein Variants Comment Organism
R297A involved in substrate binding [Candida] glabrata

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information R297A mutant protein: increased apparent KM-values for ATP and FMN by about 5 and 3times, respectively, compared to the wild-type enzyme [Candida] glabrata
0.00076
-
FMN
-
[Candida] glabrata
0.0107
-
ATP
-
[Candida] glabrata

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
[Candida] glabrata

Organism

Organism UniProt Comment Textmining
[Candida] glabrata Q6FNA9
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-Sepharose affinity chromatography, anion exchange chromatography, hydrophobic interaction chromatography, gel filtration [Candida] glabrata

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMN + ATP
-
[Candida] glabrata FAD + diphosphate
-
?

Subunits

Subunits Comment Organism
monomer crystal structure, gel filtration [Candida] glabrata

Synonyms

Synonyms Comment Organism
FMN adenylyltransferase
-
[Candida] glabrata

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.087
-
ATP
-
[Candida] glabrata
0.087
-
FMN
-
[Candida] glabrata