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1.1.1.3: homoserine dehydrogenase

This is an abbreviated version!
For detailed information about homoserine dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.3

Reaction

L-homoserine
+
NAD(P)+
=
L-aspartate 4-semialdehyde
 +
NAD(P)H
 +
H+

Synonyms

AK-HDH, AK-HSD-1, AK-HSDH, AK-HseDH, aspartate kinase-homoserine dehydrogenase, aspartokinase-homoserine dehydrogenase I, bifunctional aspartate kinase-homoserine dehydrogenase, BsHSD, HDH, hom, hom-1, Hom6, homoserine dehydrogenase 1, homoserine dehydrogenase 2, HSD, HSDH, HseDH, More, orf19.2951, PbHSD, SACOL1362, StHSD, thrA, TM_0547, TTHA0489, TtHSD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.3 homoserine dehydrogenase

Crystallization

Crystallization on EC 1.1.1.3 - homoserine dehydrogenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
for the purified ligand-free recombinant wild-type enzyme: sitting drop vapor diffusion method, mixing of 0.001 ml of 12.0 mg/ml protein solution with an equal volume of mother liquor composed of 0.1 M potassium phosphate, pH 6.2, and 20% MPD, 2 days, 20°C, for the homoserine-bound K57A mutant enzyme: sitting drop vapor diffusion method, mixing of 0.002 ml of 10 mg/ml protein solution containing 1 mM homoserine with 0.002 ml of mother liquor containing 16% polyethylene glycol monomethyl ether 2000 and 0.1 M citrate buffer, pH 6.5, 7 days, 20°C, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement and modelling
10 mg/ml purified recombinant enzyme, in TAPS, pH 8.5, in complex with inhibitor 4,4'-thiobis[2-(1-methylethyl)-phenol] in a molar ratio of 1:1, precipitant solution contains either 0.1 CHES, pH 9.5, 35% PEG 600 or 0.1 M CHES, pH 8.5, 40% PEG 400, and 0.2 M NaCl, 0.005 ml protein complex solution are equilibrated against 0.7 ml of precipitant solution using sitting drop technique, 3 months, X-ray diffraction structure determination and analysis at 3.0 A resolution, modeling
-
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, hanging drop and sitting drop methods of vapour diffusion, 8 mg/ml protein solution is mixed with reservoir solution, different conditions involving addition of 0.2 M magnesium acetate and PEG 3350 or 8000, and 3.5% glycerol, overview. X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
purified enzyme, crystallization at different pH values in the range of pH 6.0-8.5, X-ray diffraction structure determination and analysis at 2.1-2.2 A resolution
purified enzyme StHSD complexed with cysteine and NAD+, hanging drop vapour diffusion method, mixing of 0.002 ml of 5 mg/ml protein solution with 0.002 ml of reservoir solution containing 23% w/v PEG 3350, 0.2 M di-ammonium tartrate, 0.001 ml of 20 mM NAD+, and 0.001 ml of 100 mM cysteine, and equilibration against 0.1 ml of reservoir solution, 12°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement using the StHSD structure (PDB ID 4YDR) as an initial phasing model
purified recombinant enzyme in oxidized and in reduced form, hanging drop vapor diffusion method, for the oxidized form: mixing of 0.0015 ml of 5.9 mg/ml protein solution with 0.0015 ml of reservoir solution, pH 4.1, containing 9.5% w/v PEG 3350, 19% w/v PEG 400, 0.19 M magnesium chloride, and 2.5% DMSO, for the reduced form: soaking of the oxidized enzyme crystals in a solution consisting of 0.003 ml of reservoir solution and 0.001 ml of 200 mM DTT for 60 min prior to the first diffraction data collection, 12°C, X-ray diffraction structure determmination and analysis at 1.60-1.83 A resolution, molecular replacement and modelling
purified wild-type homoserine dehydrogenase in apoform, complexed with L-homoserine and NADPH in a closed form, and enzyme mutants K99A and K195A complexed with L-Hse and NADP+, hanging-drop vapour-diffusion method, mixing of 0.002 ml of 5 mg/ml protein in 5 mM Tris-HCl, pH 7.5, and in case of the ligand complex forms 15 mM of each ligand, with 0.002 ml of reservoir solution containing 3.3-4.0 M sodium formate and 50 mM CAPS, pH 10.0, X-ray diffraction structure determination and analysis at 1.83 A, 2.00 A, 1.87 A, and 1.93 A resolution, respectively, molecular replacement method using the TtHSDx02L-Hse structure (PDB ID 5XDF) as the search model