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Literature summary for 4.3.3.6 extracted from

  • Raschle, T.; Amrhein, N.; Fitzpatrick, T.B.
    On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis (2005), J. Biol. Chem., 280, 32291-32300.
    View publication on PubMed
Search for more literature for 4.3.3.6

Cloned(Commentary)

Cloned (Comment) Organism
-
 Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
acivicin inhibition of the glutaminase domain YuaaD, and thus pyridoxal 5'-phosphate synthesis Bacillus subtilis

KM Value [mM]

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

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bacillus subtilis

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bacillus subtilis

kcat/KM [mM/s]

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