Literature summary for 3.1.3.102 extracted from

Sandoval, F.J.; Roje, S.
An FMN hydrolase is fused to a riboflavin kinase homolog in plants (2005), J. Biol. Chem., 280, 38337-38345.

Search for more literature for 3.1.3.102

Activating Compound

Activating Compound	Comment	Organism	Structure
Tween 20	enzyme activity increases and temperature optimum shifts to 510°C higher temperature in the presence of Tween 20	Arabidopsis thaliana

Cloned(Commentary)

Cloned (Comment)	Organism
functional overexpression of the individual domains in Escherichia coli establishes that the riboflavin kinase and FMN hydrolase activities reside, respectively, in the C-terminal (AtFMN) and N-terminal (AtFHy) domains of the bifunctional riboflavin kinase/FMN phosphatase (AtFMN/FHy). Riboflavin kinase and FMN hydrolase domains of AtFMN/FHy can be physically separated, with little change in their kinetic properties	Arabidopsis thaliana

Cloned (Comment)

Organism

functional overexpression of the individual domains in Escherichia coli establishes that the riboflavin kinase and FMN hydrolase activities reside, respectively, in the C-terminal (AtFMN) and N-terminal (AtFHy) domains of the bifunctional riboflavin kinase/FMN phosphatase (AtFMN/FHy). Riboflavin kinase and FMN hydrolase domains of AtFMN/FHy can be physically separated, with little change in their kinetic properties

Arabidopsis thaliana

Inhibitors

Inhibitors	Comment	Organism	Structure
EDTA	the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase greatly decreases when EDTA replaced Mg2+ in the assays	Arabidopsis thaliana
phosphate	the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase is inhibited	Arabidopsis thaliana

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0008	-	FMN	pH 7.5, 30°C	Arabidopsis thaliana

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	the FMN hydrolase activity of the bifunctional riboflavin kinase/FMN phosphatase greatly decreases when EDTA replaced Mg2+ in the assays	Arabidopsis thaliana

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
25700	-	FMN hydrolase domains of the bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE	Arabidopsis thaliana
42100	-	-	Arabidopsis thaliana
43600	-	bifunctional riboflavin kinase/FMN phosphatase, gel filtration	Arabidopsis thaliana

Organism

Organism	UniProt	Comment	Textmining
Arabidopsis thaliana	Q84MD8	bifunctional riboflavin kinase/FMN phosphatase	-
Arabidopsis thaliana ecotype Columbia	Q84MD8	bifunctional riboflavin kinase/FMN phosphatase	-

Purification (Commentary)

Purification (Comment)	Organism
-	Arabidopsis thaliana

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
FMN + H2O	-	Arabidopsis thaliana	riboflavin + phosphate	-	?
FMN + H2O	-	Arabidopsis thaliana ecotype Columbia	riboflavin + phosphate	-	?

Subunits

Subunits	Comment	Organism
monomer	1 * 42100, bifunctional riboflavin kinase/FMN phosphatase, SDS-PAGE	Arabidopsis thaliana

Synonyms

Synonyms	Comment	Organism
At4g21470	gene name, bifunctional riboflavin kinase/FMN phosphatase	Arabidopsis thaliana
AtFMN/FHy	bifunctional riboflavin kinase/FMN phosphatase	Arabidopsis thaliana

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Arabidopsis thaliana

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.822	-	FMN	pH 7.5, 30°C	Arabidopsis thaliana

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.5	-	-	Arabidopsis thaliana

pH Range

pH Minimum	pH Maximum	Comment	Organism
5	8	pH 5.0: about 90% of maximal activity, pH 8.0: about 60% of maximal activity	Arabidopsis thaliana

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
1028	-	FMN	pH 7.5, 30°C	Arabidopsis thaliana