BRENDA - Enzyme Database show
show all sequences of 4.3.3.6

It takes two to Tango: Defining an essential second active site in pyridoxal 5'-phosphate synthase

Moccand, C.; Kaufmann, M.; Fitzpatrick, T.; PLoS ONE 6, e16042 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
Pdx1 and Pdx2 with and without His-tag expressed
Bacillus subtilis
Engineering
Amino acid exchange
Commentary
Organism
E105D
Pdx1
Bacillus subtilis
H115A
Pdx1
Bacillus subtilis
H115A/R138A
Pdx1
Bacillus subtilis
H170N
Pdx2, catalytically inert
Bacillus subtilis
K187A
Pdx1, 84% of wild-type activity
Bacillus subtilis
R138A
Pdx1
Bacillus subtilis
R288A
Pdx1, able to activate Pdx2
Bacillus subtilis
R288K
Pdx1, able to activate Pdx2
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.026
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.032
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.035
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.04
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C; pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.043
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C; pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.044
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.122
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.155
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.186
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.195
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.22
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.229
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.249
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.262
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.267
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.307
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.93
-
L-glutamine
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.12
-
L-glutamine
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.16
-
L-glutamine
Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C; Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
1.2
-
L-glutamine
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.31
-
L-glutamine
Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.33
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.44
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.54
-
L-glutamine
Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32830
-
unmodified Pdx1, ESI-MS
Bacillus subtilis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Purification (Commentary)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + L-glutamine
in the presence of Pdx1 and Pdx2
726269
Bacillus subtilis
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0001
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00013
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0002
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C; pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0005
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C; pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00055
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0006
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.00062
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.022
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.024
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.026
-
L-glutamine
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0295
-
L-glutamine
Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0305
-
L-glutamine
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0307
-
L-glutamine
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
Pdx1 and Pdx2 with and without His-tag expressed
Bacillus subtilis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
E105D
Pdx1
Bacillus subtilis
H115A
Pdx1
Bacillus subtilis
H115A/R138A
Pdx1
Bacillus subtilis
H170N
Pdx2, catalytically inert
Bacillus subtilis
K187A
Pdx1, 84% of wild-type activity
Bacillus subtilis
R138A
Pdx1
Bacillus subtilis
R288A
Pdx1, able to activate Pdx2
Bacillus subtilis
R288K
Pdx1, able to activate Pdx2
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.026
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.032
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.035
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.04
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C; pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.043
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C; pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.044
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.122
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.155
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.186
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.195
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.22
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.229
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.249
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.262
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.267
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.307
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.93
-
L-glutamine
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.12
-
L-glutamine
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.16
-
L-glutamine
Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C; Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
1.2
-
L-glutamine
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.31
-
L-glutamine
Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.33
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.44
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
1.54
-
L-glutamine
Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32830
-
unmodified Pdx1, ESI-MS
Bacillus subtilis
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + L-glutamine
in the presence of Pdx1 and Pdx2
726269
Bacillus subtilis
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0001
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00013
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0002
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C; pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0005
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C; pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00055
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0006
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.00062
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.022
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.024
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.026
-
L-glutamine
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0295
-
L-glutamine
Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0305
-
L-glutamine
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0307
-
L-glutamine
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00033
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00058
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00077
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00093
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0019
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0023
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0023
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.003
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0032
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0038
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0039
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0041
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0046
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0058
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.015
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0154
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.016
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.017
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0172
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.018
-
L-glutamine
Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0192
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.021
-
L-glutamine
Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.024
-
L-glutamine
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.026
-
L-glutamine
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.033
-
L-glutamine
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00033
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00058
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00077
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.00093
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0019
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0023
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0023
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.003
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0032
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0038
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0039
-
glyceraldehyde 3-phosphate
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0041
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0046
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0058
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.015
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.0154
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.016
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A/R138A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, His-tagged R138A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.017
-
L-glutamine
Pdx2 glutaminase activity, His-tagged H115A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0172
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.018
-
L-glutamine
Pdx2 glutaminase activity, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.0192
-
D-ribose 5-phosphate
pyridoxal 5'-phosphate formation, His-tagged K187A mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.021
-
L-glutamine
Pdx2 glutaminase activity, His-tagged wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.024
-
L-glutamine
Pdx2 glutaminase activity, His-tagged E105D mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
0.026
-
L-glutamine
Pdx2 glutaminase activity, R288A mutant Pdx1 protein, pH 7.5, 37°C; Pdx2 glutaminase activity, wild-type protein, pH 7.5, 37°C
Bacillus subtilis
0.033
-
L-glutamine
Pdx2 glutaminase activity, R288K mutant Pdx1 protein, pH 7.5, 37°C
Bacillus subtilis
Other publictions for EC 4.3.3.6
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748203
Smith
Crystal structures capture th ...
Geobacillus kaustophilus
J. Biol. Chem.
290
5226-5239
2015
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730418
Belitsky
Role of PdxR in the activation ...
Listeria monocytogenes
Mol. Microbiol.
92
1113-1128
2014
1
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724239
Reeksting
Exploring inhibition of Pdx1, ...
Plasmodium falciparum
Biochem. J.
449
175-187
2013
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1
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5
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5
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729134
Kim
Crystal structure of Mycobacte ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Biochem. Biophys. Res. Commun.
435
255-259
2013
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4
4
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729433
Itagaki
Differences in the roles of a ...
Bacillus circulans, Bacillus circulans SANK 72073, Bacillus subtilis
Biosci. Biotechnol. Biochem.
77
1481-1485
2013
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2
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2
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721233
Yoon
Overexpression, crystallizatio ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Acta Crystallogr. Sect. F
68
440-442
2012
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9
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723192
Matsuura
Crystal structure of pyridoxal ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
Mol. Cells
34
407-412
2012
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1
1
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726499
Guedez
Assembly of the eukaryotic PLP ...
Plasmodium berghei, Plasmodium falciparum
Structure
20
172-184
2012
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2
2
8
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28
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28
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2
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716150
Jochmann
Positive transcriptional contr ...
Corynebacterium glutamicum, Corynebacterium glutamicum NJ0898
Microbiology
157
77-88
2011
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726269
Moccand
It takes two to Tango: Definin ...
Bacillus subtilis
PLoS ONE
6
e16042
2011
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8
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25
724219
Zhang
Structural insights into the c ...
Saccharomyces cerevisiae
Biochem. J.
432
445-450
2010
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6
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724999
Derrer
Defining the structural requir ...
Plasmodium falciparum
FEBS Lett.
584
4169-4174
2010
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714170
Wallner
Dissection of contributions fr ...
Bacillus subtilis
Biochemistry
48
1928-1935
2009
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10
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713758
Hanes
Trapping of a chromophoric int ...
Bacillus subtilis
Angew. Chem. Int. Ed. Engl.
47
2102-2105
2008
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716306
Hanes
13C NMR snapshots of the compl ...
Bacillus subtilis
Nat. Chem. Biol.
4
425-430
2008
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715491
Raschle
Reaction mechanism of pyridoxa ...
Bacillus subtilis
J. Biol. Chem.
282
6098-6105
2007
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716736
Strohmeier
Structure of a bacterial pyrid ...
Bacillus subtilis
Proc. Natl. Acad. Sci. USA
103
19284-19289
2006
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715247
Burns
Reconstitution and biochemical ...
Bacillus subtilis
J. Am. Chem. Soc.
127
3682-3683
2005
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715478
Raschle
On the two components of pyrid ...
Bacillus subtilis
J. Biol. Chem.
280
32291-32300
2005
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