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Literature summary for 4.3.3.6 extracted from

  • Strohmeier, M.; Raschle, T.; Mazurkiewicz, J.; Rippe, K.; Sinning, I.; Fitzpatrick, T.B.; Tews, I.
    Structure of a bacterial pyridoxal 5'-phosphate synthase complex (2006), Proc. Natl. Acad. Sci. USA, 103, 19284-19289.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Bacillus subtilis

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion, 3D structure of the pyridoxal 5'-phosphate synthase complex with substrate glutamine bound as well as those of the individual synthase and glutaminase subunits Pdx1 and Pdx2, respectively. The complex is made up of 24 protein units assembled like a cogwheel, a dodecameric Pdx1 to which 12 Pdx2 subunits attach. Macromolecular assembly is directed by an N-terminalalpha-helix on the synthase. Interaction with the synthase subunit leads to glutaminase activation, resulting in formation of an oxyanion hole, a prerequisite for catalysis Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P37527 and P37528 P37527: pyridoxal 5'-phosphate synthase subunit Pdx1 (pdxS), and P37528: glutaminase subunit Pdx2 (PdxT)
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Purification (Commentary)

Purification (Comment) Organism
-
Bacillus subtilis

Subunits

Subunits Comment Organism
More the pyridoxal 5'-phosphate synthase complex is made up of 24 protein units assembled like a cogwheel, a dodecameric Pdx1 to which 12 Pdx2 subunits attach. Macromolecular assembly is directed by an N-terminalalpha-helix on the synthase. Interaction with the synthase subunit leads to glutaminase activation, resulting in formation of an oxyanion hole, a prerequisite for catalysis Bacillus subtilis

Synonyms

Synonyms Comment Organism
PLP synthase
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Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
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assay at Bacillus subtilis