4.3.3.6 D26A/K83A/K151A no formation of an internal chromophore with characteristic absorbance at 320 nm during reaction (observed with wild type protein) 724239 4.3.3.6 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 714170 4.3.3.6 DELTA 270-301 mainly monomer, Pdx2 activation, no pyridoxal 5'-phosphate synthesis 724999 4.3.3.6 DELTA 273-301 dodecamer, Pdx2 activation, no pyridoxal 5'-phosphate synthesis 724999 4.3.3.6 DELTA 279-301 dodecamer, Pdx2 activation, reduced pyridoxal 5'-phosphate synthesis 724999 4.3.3.6 DELTA 287-301 dodecamer, Pdx2 activation, precipitates upon addition of glyceraldehyd 3-phosphate 724999 4.3.3.6 DELTA 293-301 behaviour like DELTA 287-301 724999 4.3.3.6 DELTA 295-301 behaviour like DELTA 287-301 724999 4.3.3.6 E105D Pdx1 726269 4.3.3.6 E116A activity as the wild-type protein 724219 4.3.3.6 E136A/R139A/R140A formation of an internal chromophore with characteristic absorbance at 320 nm during reaction (also observed with wild type protein) 724239 4.3.3.6 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) 714170 4.3.3.6 E48A mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) 714170 4.3.3.6 H115A Pdx1 726269 4.3.3.6 H115A/R138A Pdx1 726269 4.3.3.6 H170N catalytically incompetent mutant of glutaminase subunit Pdx2 715491 4.3.3.6 H170N Pdx2, catalytically inert 726269 4.3.3.6 H170N site-directed mutagenesis -, 729134 4.3.3.6 H196N Pdx2, catalytically inactive 726499 4.3.3.6 H199N Pdx2 726499 4.3.3.6 K117A no synthesis of pyridoxal 5'-phosphate, capacity to catalyse dihydroxyacetone phosphate isomerization 724219 4.3.3.6 K148A no synthesis of pyridoxal 5'-phosphate, capacity to catalyse dihydroxyacetone phosphate isomerization 724219 4.3.3.6 K149A mutant enzyme does not form an adduct with ribulose-5-phosphate 715247 4.3.3.6 K149A mutant of pyridoxal 5'-phosphate synthase subunit (Pdx1) does not form the imine adduct 715491 4.3.3.6 K149R mutant of pyridoxal 5'-phosphate synthase subunit (Pdx1) retains the ability to form the imine adduct 715491 4.3.3.6 K187A Pdx1, 84% of wild-type activity 726269 4.3.3.6 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 714170 4.3.3.6 K240A activity as the wild-type protein 724219 4.3.3.6 K81A mutant of pyridoxal 5'-phosphate synthase subunit (Pdx1) does not form the imine adduct 715491 4.3.3.6 K81R mutant of pyridoxal 5'-phosphate synthase subunit (Pdx1) does not form the imine adduct 715491 4.3.3.6 L82A Pdx1 726499 4.3.3.6 M103A Pdx1 726499 4.3.3.6 M103F Pdx1 726499 4.3.3.6 M148L Pdx1 726499 4.3.3.6 M19V Pdx1 726499 4.3.3.6 M46I Pdx1 726499 4.3.3.6 additional information construction of a deletion-insertion mutant replacing both the pdxS and pdxT genes with a spectinomycin-resistance cassette, introduction into the chromosome of Listeria monocytogenes strain EGD-e. Cell growth is fully restored by addition of pyridoxal or by complementation of the mutation 730418 4.3.3.6 additional information generation of a gene btrC2 disruptant mutant strain 4-41, which shows deficiency in growth and antibiotic production, and the addition of pyridoxal to the medium restores growth and short-term antibiotics production -, 729433 4.3.3.6 additional information multiple deletion mutant proteins 724239 4.3.3.6 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) 714170 4.3.3.6 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) 714170 4.3.3.6 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) 714170 4.3.3.6 R106A mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) 714170 4.3.3.6 R135A mutant of Pdx2 (glutaminase subunit), no glutaminase activity in complex with Pdx1 (pyridoxal 5'-phosphate synthase subunit) 714170 4.3.3.6 R136A/R137A no synthesis of pyridoxal 5'-phosphate, dihydroxyacetone phosphate isomerization activity as the wild-type protein 724219 4.3.3.6 R138A Pdx1 726269 4.3.3.6 R164A completely inactive, dihydroxyacetone phosphate isomerization activity as the wild-type protein 724219 4.3.3.6 R167A reduced formation of an internal chromophore with characteristic absorbance at 320 nm during reaction (observed with wild type protein), 50% wild type activity 724239 4.3.3.6 R288A Pdx1, able to activate Pdx2 726269 4.3.3.6 R288K Pdx1, able to activate Pdx2 726269 4.3.3.6 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 724239 4.3.3.6 S270A/DELTA 273-301 dodecamer 724999 4.3.3.6 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 714170