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1.4.3.5: pyridoxal 5'-phosphate synthase

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

Word Map on EC 1.4.3.5

Reaction

pyridoxamine 5'-phosphate
+
H2O
+
O2
=
pyridoxal 5'-phosphate
+
NH3
+
H2O2

Synonyms

ePNPOx, FprA protein, oxidase, pyridoxamine phosphate, Pdx1, PDX3, PdxH, PMP oxidase, PNP oxidase, PNP/PMP oxidase, PNPO, PNPOx, PPOX, pyridox(am)ine 5'-phosphate oxidase, pyridoxal 5'-phosphate synthase, pyridoxal 5'-phosphate synthetic enzyme, pyridoxamine (pyridoxine) 5'-phosphate oxidase, pyridoxamine (pyridoxine) 5’-phosphate:O2 oxidoreductase (deaminating), pyridoxamine 5'-phosphate oxidase, pyridoxamine phosphate oxidase, pyridoxamine-5-phosphate oxidase, pyridoxamine-phosphate oxidase, pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating), pyridoxinamine 5'-phosphate oxidase, pyridoxine (pyridoxamine) 5 '-phosphate oxidase, pyridoxine (pyridoxamine) 5'-phosphate oxidase, pyridoxine (pyridoxamine) phosphate oxidase, pyridoxine 5'-phosphate oxidase, pyridoxine 5'-phosphate oxidase`, pyridoxine 5-phosphate oxidase, pyridoxine phosphate oxidase, pyridoxine-5'-phosphate oxidase, pyridoxine/pyridoxamine 5'-phosphate oxidase, pyridoxine/pyridoxamine phosphate oxidase, sgll, Sgll/PNPO, Ylr456w, Ypr172w

ECTree

     1 Oxidoreductases
         1.4 Acting on the CH-NH2 group of donors
             1.4.3 With oxygen as acceptor
                1.4.3.5 pyridoxal 5'-phosphate synthase

Crystallization

Crystallization on EC 1.4.3.5 - pyridoxal 5'-phosphate synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
5 mg/ml purified native enzyme with FMN bound in 100 mM K2PO4, pH 7.5, and 5 mM 2-mercaptoethanol, mixed with an equal volume of reservoir solution containing 60 mM HEPES, pH 6.8, and 0.65 M KH2PO4/NH4H2PO4, formation of tetragonal crystals within 4-5 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular-replacement method
enzyme in complex with pyridoxal 5'-phosphate, space group C2, 2.07 A resolution
hanging drop vapor diffusion method
structures are defined at 2.0-2.1 A resolution
-
hanging-drop and sitting-drop method, crystallized without and with an excess of pyridoxal 5'-phosphate. Structures are determined to 1.95 A and 2.65 A, respectively
-
purified recombinant enzyme from strain Rv1155, sitting drop vapour diffusion method, 9 mg/ml enzyme in 50 mM Tris-HCl, pH 8.0, 25-50 mM KF, and 10 mM glutathione, mixed with an equal volume of precipitation solution containing 0.1 M HEPES, pH 7.5, 8% ethylene glycol, and 10% PEG 8000, macroseeding with hanging drops containing equal volumes of protein and precipitation solutions overnight prior to seeding, 1-2 weeks, cryoprotection by 30% ethylene glycol, X-ray diffraction structure determination and analysis at 1.7-2.2 A, modeling
purified recombinant enzyme from strain Rv2074, sitting drop vapour diffusion method in microtiter plates at room temperature, 12 mg/ml enzyme in 50 mM Tris-HCl, pH 8.0, 5 mM DTT, and glutathione, mixed with an equal volume of precipitation solution containing 0.2 M sodium citrate, pH 5.0, 30% glycerol, and 20% PEG 4000, hanging drop vapour diffusion with 0.5 ml protein and 1 ml precipitation solutions mixed, 1-2 weeks, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.0 A, modeling
-