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Literature summary for 6.3.5.3 extracted from
- The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formation (2004), Biochemistry, 43, 10314-10327.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| PurS, smPurL, and PurQ are separately expressed in Escherichia coli | Bacillus subtilis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.181 | - |
ATP | formylglycinamide ribonucleotide amidotransferase complex | Bacillus subtilis |  |
| 0.507 | - |
formylglycinamide ribonucleotide | formylglycinamide ribonucleotide amidotransferase complex | Bacillus subtilis | |
| 1.3 | - |
L-glutamine | formylglycinamide ribonucleotide amidotransferase complex | Bacillus subtilis | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | 20 mM required for maximal activity | Bacillus subtilis | |
| Mg2+ | absolutely dependent on, 20 mM required for maximal activity | Bacillus subtilis | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus subtilis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| attempts to purify the complex resulted in separation of the constituent proteins. PurS, smPurL, and PurQ are therefore separately expressed and purified to homogeneity | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
of formylglycinamide ribonucleotide amidotransferase complex individual components | Bacillus subtilis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| formylglycinamide ribonucleotide + ATP + L-glutamine + H2O | - |
Bacillus subtilis | formylglycinamidine ribonucleotide + ADP + phosphate + L-glutamate | - |
? | |
| formylglycinamide ribonucleotide + ATP + NH3 + H2O | - |
Bacillus subtilis | formylglycinamidine ribonucleotide + ADP + phosphate | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | FGAR-AT is formed from three proteins: PurS, PurQ and smPurL. The stoichiometry of PurS/smPurL/PurQ is 2:1:1 | Bacillus subtilis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FGAR-AT | - |
Bacillus subtilis |
| formylglycinamide ribonucleotide amidotransferase complex | - |
Bacillus subtilis |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | - |
Bacillus subtilis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
activity with glutamine | Bacillus subtilis |
| 7.2 | - |
activity with NH4+ | Bacillus subtilis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | 7.5 | pH 6.5: about 40% of maximal activity, pH 7.5: about 35% of maximal activity, reaction with glutamine | Bacillus subtilis |
| 6.8 | 7.5 | pH 6.8: about 50% of maximal activity, pH 7.5: about 65% of maximal activity, reaction with NH4+ | Bacillus subtilis |
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