Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3
pyridoxal 5'-phosphate + 4 H2O + phosphate
-
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
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
in the presence of Pdx1 and Pdx2
-
-
?
D-ribulose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
?
-
preference of D-ribose 5-phosphate compared to D-ribulose 5-phosphate
-
-
?
L-glutamine + H2O
L-glutamate + 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. 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
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of ribose 5-phosphate and glyceraldehyde 3-phosphate to pyridoxal 5'-phosphate
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
the enzyme is involved in vitamin B6 biosynthesis
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
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
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
mechanistic studies. Pdx2 has glutaminase activity and channels ammonia to the active site of the PLP synthase subunit, Pdx1, where ribose-5-phosphate, glyceraldehyde-3-phosphate, and ammonia are condensed in a complex series of reactions. Under pre-steady-state conditions, a chromophoric intermediate is observed that accumulates upon addition of only two of the substrates, D-ribose 5-phosphate and glutamine. The intermediate is covalently bound to the protein. The phosphate unit of R5P is eliminated rather than hydrolyzed in route to intermediate formation
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
preference of D-ribose 5-phosphate compared to D-ribulose 5-phosphate. Characterization of a novel chromophoric reaction intermediate. The chromophoric group of this intermediate is appended to the epsilon-amino group of Lys81 and that the new residue has the composition C5H6O2, corresponding to the elimination of one equivalent of inorganic phosphate, one molecule of water one additional proton from the original protonated imine adduct
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
the ammonia generated at the YaaE active site is channelled to the active site of YaaD where pyridoxal 5'-phosphate formation occurs
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
the synthase subunit of this enzyme, Pdx1, operates in concert with the glutaminase subunit, Pdx2, to catalyze the complex condensation of ribose 5-phosphate, glutamine and glyceraldehyde 3-phosphate to form pyridoxal 5'-phosphate. Many if not all of the reaction intermediates are covalently bound to the synthase subunit, thus making them difficult to isolate and characterize. By denaturing the enzyme at points along the reaction coordinate, the structures of three covalently bound intermediates are solved. Thes analysis reveals a 1,5 migration of the lysine amine linking the intermediate to the enzyme during the conversion of ribose 5-phosphate to pyridoxal 5'-phosphate
-
-
?
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.077
D-glyceraldehyde 3-phosphate
-
pH 8.0, 37°C
0.026 - 0.185
D-ribose 5-phosphate
0.155 - 0.307
glyceraldehyde 3-phosphate
0.026
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
0.032
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
0.035
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
0.04
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
0.04
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
0.043
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
0.043
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
0.044
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
0.068
D-ribose 5-phosphate
-
pH 8.0, 37°C
0.122
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
0.126
D-ribose 5-phosphate
-
pH 8.0, 37°C, wild-type enzyme
0.185
D-ribose 5-phosphate
-
pH 8.0, 37°C, mutant enzyme K149R
0.155
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
0.186
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
0.195
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
0.22
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
0.229
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
0.249
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
0.262
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
0.267
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
0.307
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
0.93
L-glutamine
-
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
0.99
L-glutamine
-
pH 8.0, 37°C
1.12
L-glutamine
-
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
1.16
L-glutamine
-
Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C
1.16
L-glutamine
-
Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
1.2
L-glutamine
-
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C
1.31
L-glutamine
-
Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
1.33
L-glutamine
-
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
1.44
L-glutamine
-
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
1.54
L-glutamine
-
Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0001 - 0.004
D-ribose 5-phosphate
0.0007
D-ribulose 5-phosphate
-
pH 8.0, 37°C, free pyridoxal 5'-phosphate synthase subunit (Pdx1)
0.022 - 0.127
L-glutamine
0.0001
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
0.00013
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
0.0002
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
0.0002
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
0.00033
D-ribose 5-phosphate
-
pH 8.0, 37°C
0.00033
D-ribose 5-phosphate
-
pH 8.0, 37°C, mutant enzyme K149R
0.0005
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
0.0005
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
0.00055
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
0.0006
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
0.00062
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
0.00067
D-ribose 5-phosphate
-
pH 8.0, 37°C, free pyridoxal 5'-phosphate synthase subunit (Pdx1)
0.004
D-ribose 5-phosphate
-
pH 8.0, 37°C, wild-type enzyme
0.022
L-glutamine
-
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
0.024
L-glutamine
-
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
0.024
L-glutamine
-
Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
0.024
L-glutamine
-
Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
0.024
L-glutamine
-
Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C
0.026
L-glutamine
-
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
0.0295
L-glutamine
-
Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
0.0305
L-glutamine
-
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C
0.0307
L-glutamine
-
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
0.127
L-glutamine
-
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0018 - 0.044
D-ribose 5-phosphate
0.00033 - 0.0039
glyceraldehyde 3-phosphate
0.016 - 0.128
L-glutamine
0.0018
D-ribose 5-phosphate
-
pH 8.0, 37°C, mutant enzyme K149R
0.0023
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
0.0038
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
0.0041
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
0.0046
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
0.0058
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
0.015
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
0.0154
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
0.0172
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
0.0192
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
0.03
D-ribose 5-phosphate
-
pH 8.0, 37°C, wild-type enzyme
0.044
D-ribose 5-phosphate
-
pH 8.0, 37°C
0.00033
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
0.00058
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
0.00077
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
0.00093
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
0.0019
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
0.0023
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
0.003
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
0.0032
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
0.0039
glyceraldehyde 3-phosphate
-
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
0.016
L-glutamine
-
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
0.016
L-glutamine
-
Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
0.017
L-glutamine
-
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
0.018
L-glutamine
-
Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
0.021
L-glutamine
-
Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C
0.024
L-glutamine
-
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
0.026
L-glutamine
-
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C
0.026
L-glutamine
-
Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
0.033
L-glutamine
-
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
0.128
L-glutamine
-
pH 8.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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)
E48A
mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit)
K149R
-
mutant of pyridoxal 5'-phosphate synthase subunit (Pdx1) retains the ability to form the imine adduct
K187A
-
Pdx1, 84% of wild-type activity
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
K81A
-
mutant of pyridoxal 5'-phosphate synthase subunit (Pdx1) does not form the imine adduct
K81R
-
mutant of pyridoxal 5'-phosphate synthase subunit (Pdx1) does not form the imine adduct
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)
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)
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)
R106A
mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit)
R135A
mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit)
R288A
-
Pdx1, able to activate Pdx2
R288K
-
Pdx1, able to activate Pdx2
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
H170N
-
catalytically incompetent mutant of glutaminase subunit Pdx2
H170N
-
Pdx2, catalytically inert
K149A
-
mutant enzyme does not form an adduct with ribulose-5-phosphate
K149A
-
mutant of pyridoxal 5'-phosphate synthase subunit (Pdx1) does not form the imine adduct
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hanes, J.W.; Keresztes, I.; Begley, T.P.
Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis of pyridoxal 5'-phosphate
Angew. Chem. Int. Ed. Engl.
47
2102-2105
2008
Bacillus subtilis
brenda
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
Biochemistry
48
1928-1935
2009
Bacillus subtilis (O31465), Bacillus subtilis
brenda
Burns, K.E.; Xiang, Y.; Kinsland, C.L.; McLafferty, F.W.; Begley, T.P.
Reconstitution and biochemical characterization of a new pyridoxal-5'-phosphate biosynthetic pathway
J. Am. Chem. Soc.
127
3682-3683
2005
Bacillus subtilis
brenda
Raschle, T.; Amrhein, N.; Fitzpatrick, T.B.
On the two components of pyridoxal 5'-phosphate synthase from Bacillus subtilis
J. Biol. Chem.
280
32291-32300
2005
Bacillus subtilis
brenda
Raschle, T.; Arigoni, D.; Brunisholz, R.; Rechsteiner, H.; Amrhein, N.; Fitzpatrick, T.B.
Reaction mechanism of pyridoxal 5'-phosphate synthase. Detection of an enzyme-bound chromophoric intermediate
J. Biol. Chem.
282
6098-6105
2007
Bacillus subtilis
brenda
Hanes, J.W.; Keresztes, I.; Begley, T.P.
13C NMR snapshots of the complex reaction coordinate of pyridoxal phosphate synthase
Nat. Chem. Biol.
4
425-430
2008
Bacillus subtilis
brenda
Strohmeier, M.; Raschle, T.; Mazurkiewicz, J.; Rippe, K.; Sinning, I.; Fitzpatrick, T.B.; Tews, I.
Structure of a bacterial pyridoxal 5'-phosphate synthase complex
Proc. Natl. Acad. Sci. USA
103
19284-19289
2006
Bacillus subtilis (P37527 and P37528)
brenda
Moccand, C.; Kaufmann, M.; Fitzpatrick, T.
It takes two to Tango: Defining an essential second active site in pyridoxal 5'-phosphate synthase
PLoS ONE
6
e16042
2011
Bacillus subtilis
brenda
Itagaki, S.; Haga, M.; Oikawa, Y.; Sakoda, A.; Ohke, Y.; Sawada, H.; Eguchi, T.; Tamegai, H.
Differences in the roles of a glutamine amidotransferase subunit of pyridoxal 5'-phosphate synthase between Bacillus circulans and Bacillus subtilis
Biosci. Biotechnol. Biochem.
77
1481-1485
2013
Bacillus subtilis, Niallia circulans (Q8L1A7), Niallia circulans (Q8L1A8), Niallia circulans SANK 72073 (Q8L1A7), Niallia circulans SANK 72073 (Q8L1A8)
brenda