Literature summary extracted from
Wallner, S.; Neuwirth, M.; Flicker, K.; Tews, I.; Macheroux, P.
Dissection of contributions from invariant amino acids to complex formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase complex from Bacillus subtilis (2009), Biochemistry, 48, 1928-1935.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.3.3.6 |
expression in Escherichia coli |
Bacillus subtilis |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
4.3.3.6 |
D99A |
mutant of Pdx1 (pyridoxal 5'-phosphate synthase subunit), 5% of the pyridoxal 5'-phosphate synthase activity compared to wild-type enzyme with L-glutamine as N-donor, 17.2% of the glutaminase activity compared to wild-type enzyme |
Bacillus subtilis |
4.3.3.6 |
E15A |
mutant of Pdx2 (glutaminase subunit), 280% of the glutaminase activity compared to wild-type activity, Pdx2 (glutaminase subunit) complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) |
Bacillus subtilis |
4.3.3.6 |
E48A |
mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) |
Bacillus subtilis |
4.3.3.6 |
K18A |
mutant of Pdx1 (pyridoxal 5'-phosphate synthase subunit), 40.5% of the pyridoxal 5'-phosphate synthase activity compared to wild-type enzyme with L-glutamine as N-donor, 64.5% of the glutaminase activity compared to wild-type enzyme |
Bacillus subtilis |
4.3.3.6 |
Q10A |
mutant of Pdx2 (glutaminase subunit), 94% of the glutaminase activity compared to wild-type activity, Pdx2 (glutaminase subunit) complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) |
Bacillus subtilis |
4.3.3.6 |
Q10E |
mutant of Pdx2 (glutaminase subunit), 2% of the glutaminase activity compared to wild-type activity, Pdx2 (glutaminase subunit) complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) |
Bacillus subtilis |
4.3.3.6 |
Q10N |
mutant of Pdx2 (glutaminase subunit), 34% of the glutaminase activity compared to wild-type activity, Pdx2 (glutaminase subunit) complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) |
Bacillus subtilis |
4.3.3.6 |
R106A |
mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) |
Bacillus subtilis |
4.3.3.6 |
R135A |
mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) |
Bacillus subtilis |
4.3.3.6 |
S75A |
mutant of Pdx1 (pyridoxal 5'-phosphate synthase subunit), 51% of the pyridoxal 5'-phosphate synthase activity compared to wild-type enzyme with L-glutamine as N-donor, 84% of the glutaminase activity compared to wild-type enzyme |
Bacillus subtilis |
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.3.3.6 |
Bacillus subtilis |
O31465 |
Pdx2, glutaminase subunit |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.3.3.6 |
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine |
L-glutamine binding triggers a cascade of conformational changes of Pdx2 (glutaminase subunit) that leads to a structure favorable for Pdx1 (pyridoxal 5'-phosphate synthase subunit) binding |
Bacillus subtilis |
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate |
- |
? |
|
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
4.3.3.6 |
37 |
- |
assay |
Bacillus subtilis |