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Literature summary for 2.7.1.26 extracted from
- An FMN hydrolase is fused to a riboflavin kinase homolog in plants (2005), J. Biol. Chem., 280, 38337-38345.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the 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 AtFMN/FHy | Arabidopsis thaliana |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0000103 | - |
riboflavin | bifunctional enzyme AtFMN/FHy | Arabidopsis thaliana |  |
| 0.0002 | - |
ATP | bifunctional enzyme AtFMN/FHy | Arabidopsis thaliana | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
ecotype Columbia | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + riboflavin | - |
Arabidopsis thaliana | ADP + FMN | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AtFMN/FHy | bifunctional enzyme has riboflavin kinase and FMN hydrolase activities | Arabidopsis thaliana |
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