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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.
    View publication on PubMed

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
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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
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 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.3.6 37
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 assay Bacillus subtilis