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4.3.3.6: pyridoxal 5'-phosphate synthase (glutamine hydrolysing)

This is an abbreviated version!
For detailed information about pyridoxal 5'-phosphate synthase (glutamine hydrolysing), go to the full flat file.

Word Map on EC 4.3.3.6

Reaction

D-ribose 5-phosphate
+
D-glyceraldehyde 3-phosphate
 +
L-glutamine
=
pyridoxal 5'-phosphate
 +
L-glutamate
 + 3 H2O +
phosphate

Synonyms

Pdx1, PDX2, PdxS, Ph1355, PLP synthase, PLP-synthase complex, PLPS, pyridoxal 5'-phosphate synthase, pyridoxal 5-phosphate synthase, pyridoxal 5-phosphate synthase Snz1, pyridoxal biosynthesis lyase, pyridoxal biosynthesis lyase PdxS, Rv2606c, Snz1

ECTree

     4 Lyases
         4.3 Carbon-nitrogen lyases
             4.3.3 Amine-lyases
                4.3.3.6 pyridoxal 5'-phosphate synthase (glutamine hydrolysing)

Engineering

Engineering on EC 4.3.3.6 - pyridoxal 5'-phosphate synthase (glutamine hydrolysing)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
E105D
-
Pdx1
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)
H115A
-
Pdx1
H115A/R138A
-
Pdx1
H170N
K149A
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)
R138A
-
Pdx1
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
D26A/K83A/K151A
-
no formation of an internal chromophore with characteristic absorbance at 320 nm during reaction (observed with wild type protein)
DELTA 270-301
mainly monomer, Pdx2 activation, no pyridoxal 5'-phosphate synthesis
DELTA 273-301
dodecamer, Pdx2 activation, no pyridoxal 5'-phosphate synthesis
DELTA 279-301
dodecamer, Pdx2 activation, reduced pyridoxal 5'-phosphate synthesis
DELTA 287-301
dodecamer, Pdx2 activation, precipitates upon addition of glyceraldehyd 3-phosphate
DELTA 293-301
behaviour like DELTA 287-301
DELTA 295-301
behaviour like DELTA 287-301
E136A/R139A/R140A
-
formation of an internal chromophore with characteristic absorbance at 320 nm during reaction (also observed with wild type protein)
H196N
-
Pdx2, catalytically inactive
R167A
-
reduced formation of an internal chromophore with characteristic absorbance at 320 nm during reaction (observed with wild type protein), 50% wild type activity
R85A/H88A/E91A
-
no formation of an internal chromophore with characteristic absorbance at 320 nm during reaction (observed with wild type protein), dodecameric assembly prevented
S270A/DELTA 273-301
dodecamer
E116A
activity as the wild-type protein
K117A
no synthesis of pyridoxal 5'-phosphate, capacity to catalyse dihydroxyacetone phosphate isomerization
K148A
no synthesis of pyridoxal 5'-phosphate, capacity to catalyse dihydroxyacetone phosphate isomerization
K240A
activity as the wild-type protein
R136A/R137A
no synthesis of pyridoxal 5'-phosphate, dihydroxyacetone phosphate isomerization activity as the wild-type protein
R164A
completely inactive, dihydroxyacetone phosphate isomerization activity as the wild-type protein
additional information