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Literature summary for 2.7.7.2 extracted from

  • Leone, P.; Galluccio, M.; Brizio, C.; Barbiroli, A.; Iametti, S.; Indiveri, C.; Barile, M.
    The hidden side of the human FAD synthase 2 (2019), Int. J. Biol. Macromol., 138, 986-995 .
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
reduced glutathione stimulates FAD hydrolysis Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
KI inhibits FAD hydrolysis Homo sapiens
NADH inhibits FAD hydrolysis Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ Co2+ induces FAD hydrolysis, which is strongly stimulated in the presence of K+, K0.5 value is 0.035 mM Homo sapiens
K+ stimulates Co2+-induced FAD hydrolysis, K0.5 value 7.2 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + FMN
-
Homo sapiens diphosphate + FAD
-
r
diphosphate + FAD
-
Homo sapiens ATP + FMN
-
r
additional information enzyme contains an N-terminal molybdopterin-binding resembling domain with FAD hydrolytic activity in presence of both Co2+ and chemical mercurial reagents Homo sapiens ?
-
-

Synonyms

Synonyms Comment Organism
FADS2
-
Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
hydrolysis of FAD Homo sapiens