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Information on EC 4.3.3.6 - pyridoxal 5'-phosphate synthase (glutamine hydrolysing)
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4.3.3.6 pyridoxal 5'-phosphate synthase (glutamine hydrolysing)IUBMB Comments
The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. The enzyme complex is found in aerobic bacteria, archaea, fungi and plants.
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Word Map
- 4.3.3.6
- glutaminase
- ammonia
-
amidotransferase
-
heteromeric
- deoxyxylulose
-
vitamer
- pentose
- falciparum
- ribulose
- malaria
- eubacteria
-
dodecameric
- imine
-
oxyanion
- l-glutamine
- triose
-
plasmodial
-
hexameric
- drug development
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
plp synthase, rv2606c, pyridoxal biosynthesis lyase, ph1355, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Pdx1
PdxS
Ph1355
PLP synthase
PLP-synthase complex
pyridoxal 5'-phosphate synthase
pyridoxal biosynthesis lyase
pyridoxal biosynthesis lyase PdxS
Rv2606c
Pdx1
-
pyridoxal 5'-phosphate synthase complex consits of Pdx1 and Pdx2
PdxS
PdxS catalyses the condensation of ribulose 5-phosphate, glyceraldehyde 3-phosphate and ammonia, while glutamine amidotransferase (PdxT) catalyses the production of ammonia from glutamine. PdxS and PdxT form a complex
PdxS
PdxS catalyses the condensation of ribulose 5-phosphate, glyceraldehyde 3-phosphate and ammonia, while glutamine amidotransferase (PdxT) catalyses the production of ammonia from glutamine. PdxS and PdxT form a complex
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
overall reaction
-
-
-
D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + NH3 = pyridoxal 5'-phosphate + 4 H2O + phosphate
(1b)
-
-
-
L-glutamine + H2O = L-glutamate + NH3
(1a)
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-ribose 5-phosphate,D-glyceraldehyde 3-phosphate pyridoxal 5'-phosphate-lyase
The ammonia is provided by the glutaminase subunit and channeled to the active site of the lyase subunit by a 100 A tunnel. The enzyme can also use ribulose 5-phosphate and dihydroxyacetone phosphate. The enzyme complex is found in aerobic bacteria, archaea, fungi and plants.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + phosphate
D-ribulose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine
?
-
preference of D-ribose 5-phosphate compared to D-ribulose 5-phosphate
-
-
?
ribulose 5-phosphate + glyceraldehyde 3-phosphate + NH3
pyridoxal 5'-phosphate + 4 H2O + phosphate
-
-
-
?
ribulose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + 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
-
-
?
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 + D-glyceraldehyde 3-phosphate + NH3
pyridoxal 5'-phosphate + 4 H2O + phosphate
-
-
-
?
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-ribose 5-phosphate + glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
-
-
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + L-glutamine
pyridoxal 5'-phosphate + L-glutamate + 3 H2O + phosphate
in the presence of Pdx2
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + phosphate
in the absence of Pdx2
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + phosphate
-
-
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + phosphate
-
in the absence of Pdx2
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + phosphate
in the absence of Pdx2
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + phosphate
-
-
-
?
D-ribose 5-phosphate + glyceraldehyde 3-phosphate + NH4+
pyridoxal 5'-phosphate + 4 H2O + 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
-
-
?
additional information
?
-
BtrC2 shows no catalytic activity as 2-deoxy-scyllo-inosose (DOI) synthase
-
-
?
additional information
?
-
BtrC2 shows no catalytic activity as 2-deoxy-scyllo-inosose (DOI) synthase
-
-
?
additional information
?
-
Niallia circulans SANK 72073
BtrC2 shows no catalytic activity as 2-deoxy-scyllo-inosose (DOI) synthase
-
-
?
additional information
?
-
Niallia circulans SANK 72073
BtrC2 shows no catalytic activity as 2-deoxy-scyllo-inosose (DOI) synthase
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of ribose 5-phosphate and glyceraldehyde 3-phosphate to pyridoxal 5'-phosphate
-
-
?
additional information
?
-
BtrC2 shows no catalytic activity as 2-deoxy-scyllo-inosose (DOI) synthase
-
-
?
additional information
?
-
BtrC2 shows no catalytic activity as 2-deoxy-scyllo-inosose (DOI) synthase
-
-
?
additional information
?
-
Niallia circulans SANK 72073
BtrC2 shows no catalytic activity as 2-deoxy-scyllo-inosose (DOI) synthase
-
-
?
additional information
?
-
Niallia circulans SANK 72073
BtrC2 shows no catalytic activity as 2-deoxy-scyllo-inosose (DOI) synthase
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
1.0 mM Mn2+, Mg2+, Co2+, Ca2+, Ni2+, Fe3+, Fe2+, Cu3+, Cu2+, or Zn2+ has no effect on activity
additional information
a glycerol molecule is bound at the active site of the enzyme structure through interactions with the conserved residues of Asp29 and Lys86
additional information
-
a glycerol molecule is bound at the active site of the enzyme structure through interactions with the conserved residues of Asp29 and Lys86
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acivicin
-
inhibition of the glutaminase domain YuaaD, and thus pyridoxal 5'-phosphate synthesis
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PdxR
PdxR is a direct activator of the pdxST operon, has a regulatory function in de novo synthesis of pyridoxal 5'-phosphate, encoded by gene pdxR, PdxR is a member of the MocR/GabR subfamily with an N-terminal putative DNA-binding domain and a C-terminal aminotransferase-like domain. PdxR is also a negative autoregulator, and its ability to repress is increased by pyridoxal 5'-phosphate. PdxR-like proteins, for which PLP plays just a signalling role, form a separate functional group among the MocR/GabRtype proteins. Mutational analysis of the PdxR binding site, overview
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Malaria
Exploring inhibition of Pdx1, a component of the PLP synthase complex of the human malaria parasite Plasmodium falciparum.
Tuberculosis
Cloning, expression, purification, crystallization and X-ray crystallographic analysis of Rv2606c from Mycobacterium tuberculosis H37Rv.
Tuberculosis
Crystal structure of Mycobacterium tuberculosis Rv2606c: a pyridoxal biosynthesis lyase.
Tuberculosis
Transposon mutagenesis of Mycobacterium marinum identifies a locus linking pigmentation and intracellular survival.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.122
D-ribose 5-phosphate
-
pyridoxal 5'-phosphate formation, R288A mutant Pdx1 protein, pH 7.5, 37°C
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
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007
D-ribulose 5-phosphate
-
pH 8.0, 37°C, free pyridoxal 5'-phosphate synthase subunit (Pdx1)
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
0.0005
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)
0.022
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
0.00033
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
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
4-phospho-D-erythronhydrazide
Plasmodium falciparum
-
Pdx1 in the heteromeric pyridoxal 5'-phosphate synthase complex, pH 8.0, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00025
0.00031
M103A mutant Pdx1, NH4Cl as NH3+ donor, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.00042
M103A mutant Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0007
-
Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.000779
wild-type protein, in the presence of Pdx2, pH 8.0, 37°C
0.0008
M148L mutant Pdx1, NH4Cl as NH3+ donor, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0009
0.0011
Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0012
L82A mutant Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0013
0.0015
M46I mutant Pdx1, NH4Cl as NH3+ donor, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0018
M19V mutant Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.002
M19V mutant Pdx1, NH4Cl as NH3+ donor, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0028
M46I mutant Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0037
M148L mutant Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.087
M19V mutant Pdx1/Pdx2 complex, glutaminase activity, pH 8, 30°C
0.115
L82A mutant Pdx1/Pdx2 complex, glutaminase activity, pH 8, 30°C
0.126
M103F mutant Pdx1/Pdx2 complex, glutaminase activity, pH 8, 30°C
0.175
0.178
M103A mutant Pdx1/Pdx2 complex, glutaminase activity, pH 8, 30°C
0.229
M148L mutant Pdx1/Pdx2 complex, glutaminase activity, pH 8, 30°C
0.233
0.284
M46I mutant Pdx1/Pdx2 complex, glutaminase activity, pH 8, 30°C
0.00025
L82A mutant Pdx1, NH4Cl as NH3+ donor, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.00025
DELTA 279-301 protein, in the presence of Pdx2, pH 8.0, 37°C
0.0009
Pdx1, NH4Cl as NH3+ donor, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0009
Plasmodium falciparum Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0009
-
Pdx1/Plasmodium berghei Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0013
Pdx1/Plasmodium falciparum Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.0013
-
Plasmodium berghei Pdx1/Pdx2 complex, pyridoxal 5'-phosphate synthesis, pH 8, 37°C
0.175
Plasmodium falciparum Pdx1/Pdx2 complex, glutaminase activity, pH 8, 30°C
0.175
-
Pdx1/Plasmodium berghei Pdx2 complex, glutaminase activity, pH 8, 30°C
0.233
Pdx1/Plasmodium falciparum Pdx2 complex, glutaminase activity, pH 8, 30°C
0.233
-
Plasmodium berghei Pdx1/Pdx2 complex, glutaminase activity, pH 8, 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q5L3Y2: subunit PdxS, Q5L3Y1: subunit PdxT
SwissProt
brenda
gene lmo2101 or pdxS, encoding a subunit of pyridoxal 5'-phosphate synthase
UniProt
brenda