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Literature summary extracted from
- Enzymatic properties of futalosine hydrolase, an enzyme essential to a newly identified menaquinone biosynthetic pathway (2009), Biosci. Biotechnol. Biochem., 73, 1137-1141.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.2.26 | expression of maltose-binding protein fusion enzyme in Escherichia coli | Thermus thermophilus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.2.26 | hypoxanthine | product inhibition | Thermus thermophilus |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.2.26 | 0.154 | - |
futalosine | pH 4.5, 80°C | Thermus thermophilus | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.2.26 | additional information | the enzyme activity is not affected by 1 mM of EDTA, Pb2+, Fe2+, Mg2+, Ba2+, Co2+, Zn2+, Ca2+, Ni2+, Cu2+, and Mn2+ | Thermus thermophilus |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.26 | 23800 | - |
4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE | Thermus thermophilus |
| 3.2.2.26 | 66300 | - |
4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE | Thermus thermophilus |
| 3.2.2.26 | 220000 | - |
recombinant MBP-fusion TTHA0556, gel filtration | Thermus thermophilus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.2.26 | futalosine + H2O | Thermus thermophilus | - |
dehypoxanthine futalosine + hypoxanthine | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.2.26 | Thermus thermophilus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.2.26 | recombinant maltose-binding protein fusion enzyme from Escherichia coli by amylose affinity chromatography and cleavage of the tag by Factor Xa | Thermus thermophilus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.26 | additional information | - |
recombinant MBP-fusion and detagged enzymes show similar activities | Thermus thermophilus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.2.26 | futalosine + H2O | - |
Thermus thermophilus | dehypoxanthine futalosine + hypoxanthine | - |
? | |
| 3.2.2.26 | futalosine + H2O | TTHA0556 is absolutely specific for futalosine and shows no no activity with diverse other structurally related nucleotides and nucleosides, overview | Thermus thermophilus | dehypoxanthine futalosine + hypoxanthine | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.2.26 | homotetramer | 4 * 23800, detagged recombinant TTHA0556, SDS-PAGE, 4 * 66300, recombinant MBP-fusion TTHA0556, SDS-PAGE | Thermus thermophilus |
| 3.2.2.26 | More | quarternary structure, overview | Thermus thermophilus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.2.26 | MqnB | - |
Thermus thermophilus |
| 3.2.2.26 | TTHA0556 | - |
Thermus thermophilus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.26 | 80 | - |
- |
Thermus thermophilus |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.2.26 | 1.02 | - |
futalosine | pH 4.5, 80°C | Thermus thermophilus | |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.26 | 4.5 | - |
- |
Thermus thermophilus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.2.26 | 3 | 9 | - |
Thermus thermophilus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.2.26 | additional information | no cofactor required | Thermus thermophilus |
Ki Value [mM]
| EC Number | Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.2.26 | 1.1 | - |
hypoxanthine | pH 4.5, 80°C | Thermus thermophilus | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.2.2.26 | metabolism | the enzyme catalyzes the second step of the futalosine pathway starting from chorismate, alternative to the menaquinone pathway, overview | Thermus thermophilus |
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Release 2023.1 (January 2023)
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