Cloned (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
acivicin | inhibition of the glutaminase domain YuaaD, and thus pyridoxal 5'-phosphate synthesis | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.068 | - |
D-ribose 5-phosphate | pH 8.0, 37°C | Bacillus subtilis | |
0.077 | - |
D-glyceraldehyde 3-phosphate | pH 8.0, 37°C | Bacillus subtilis | |
0.99 | - |
L-glutamine | pH 8.0, 37°C | Bacillus subtilis |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | 1.0 mM Mn2+, Mg2+, Co2+, Ca2+, Ni2+, Fe3+, Fe2+, Cu3+, Cu2+, or Zn2+ has no effect on activity | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine | Bacillus subtilis | the enzyme is involved in vitamin B6 biosynthesis | pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine | the enzyme is involved in vitamin B6 biosynthesis | Bacillus subtilis | pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate | - |
? | |
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine | two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. The synthase reaction can also utilize an external ammonium source but, in contrast to other glutamine amidotransferases, is dependent on YaaE under certain conditions | Bacillus subtilis | pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate | - |
? | |
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3 | two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. Both the glutaminase and synthase reactions are dependent on the respective protein partner. The synthase reaction can also utilize an external ammonium source but, in contrast to other glutamine amidotransferases, is dependent on YaaE under certain conditions | Bacillus subtilis | pyridoxal 5'-phosphate + 4 H2O + phosphate | - |
? | |
L-glutamine + H2O | two proteins form a complex that functions as a glutamine amidotransferase, with YaaE as the glutaminase domain and YaaD as the acceptor and pyridoxal 5'-phosphate synthesis domain. Glutaminase activity of YaaE is only detected in the presence of its partner protein YaaD. A 1:1 stoichiometry of both proteins appears to be optimal for activity | Bacillus subtilis | L-glutamate + NH3 | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Bacillus subtilis |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.00033 | - |
D-ribose 5-phosphate | pH 8.0, 37°C | Bacillus subtilis | |
0.127 | - |
L-glutamine | pH 8.0, 37°C | Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Bacillus subtilis |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.044 | - |
D-ribose 5-phosphate | pH 8.0, 37°C | Bacillus subtilis | |
0.128 | - |
L-glutamine | pH 8.0, 37°C | Bacillus subtilis |