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Literature summary for 1.4.3.5 extracted from

  • Raschle, T.; Speziga, D.; Kress, W.; Moccand, C.; Gehrig, P.; Amrhein, N.; Weber-Ban, E.; Fitzpatrick, T.B.
    Intersubunit cross-talk in pyridoxal 5-phosphate synthase, coordinated by the C terminus of the synthase subunit (2009), J. Biol. Chem., 284, 7706-7718.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.5

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
DELTA273-294 a deletion mutant lacking the C-terminal 22 amino acids shows that the C-terminus is essential for enzymatic activity Bacillus subtilis
DELTAW294 a deletion mutant in which only the C-terminal tryptophan is deleted, displays activity similar to the wild type protein for chromophore and pyridoxal formation Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31480
-
 ESI-mass spectrometry Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information at the Pdx1 active site, a pentose phosphate and triose phosphate sugar (i.e. ribose 5-phosphate and glyceraldehyde 3-phosphate) are combined along with ammonia to form pyridoxal Bacillus subtilis ?
-
 ?

Synonyms

Synonyms Comment Organism
Pdx1
-
 Bacillus subtilis
pyridoxal 5'-phosphate synthase
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Bacillus subtilis

General Information

General Information Comment Organism
physiological function a glutamine amidotransferase consisting of the synthase Pdx1 and its glutaminase partner, Pdx2, form a complex that directly synthesizes pyridoxal from ribose 5-phosphate, glyceraldehyde 3-phosphate, and glutamine. The protein complex displays an ornate architecture consisting of 24 subunits, two hexameric rings of 12 Pdx1 subunits to which 12 Pdx2 subunits attach, with the glutaminase and synthase active sites remote from each other Bacillus subtilis
physiological function fluorescence spectrophotometry is used to demonstrate that the Pdx1 C-terminus is indispensable for pyridoxal synthase activity and mediates intersubunit cross-talk within the enzyme complex. The C-terminus can act as a flexible lid, bridging as well as shielding the active site of an adjacent protomer in Pdx1. Ribose 5-phosphate binding triggers strong cooperativity in Pdx1, and the affinity for this substrate is substantially enhanced upon interaction with the Michaelis complex of Pdx2 and glutamine Bacillus subtilis