1.2.1.11: aspartate-semialdehyde dehydrogenase
This is an abbreviated version!
For detailed information about aspartate-semialdehyde dehydrogenase, go to the full flat file.
Word Map on EC 1.2.1.11
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1.2.1.11
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diaminopimelate
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aspartokinase
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dihydrodipicolinate
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balanced-lethal
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beta-aspartyl
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drug development
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medicine
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biotechnology
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pharmacology
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synthesis
- 1.2.1.11
- diaminopimelate
- aspartokinase
- dihydrodipicolinate
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balanced-lethal
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beta-aspartyl
- drug development
- medicine
- biotechnology
- pharmacology
- synthesis
Reaction
Synonyms
AFUA_3G06830, ASA dehydrogenase, ASA DH, ASA-DH, ASADH, ASADHD, Asd, ASD enzyme, Asd1, Asd2, AsdA, aspartate beta-semialdehyde dehydrogenase, aspartate semialdehyde dehydrogenase, aspartate-beta-semialdehyde dehydrogenase, aspartate-beta-semialdeyhyde dehydrogenase, aspartate-semialdehyde dehydrogenase, aspartic acid semialdehyde dehydrogenase, aspartic beta-semialdehyde dehydrogenase, aspartic semialdehyde dehydrogenase, aspartyl beta-semialdehyde dehydrogenase, aspartyl semialdehyde dehydrogenase, BDCG_01946, CNA02450, dehydrogenase, aspartate semialdehyde, ecASADH, FtASADH, hiASADH, L-aspartate-beta-semialdehyde dehydrogenase, L-aspartate-beta-semialdehyde:NADP oxidoreductase (phosphorylating), Rv3708c
ECTree
1.2.1.11 aspartate-semialdehyde dehydrogenaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 1.2.1.11 - aspartate-semialdehyde dehydrogenase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
purified recombinant C-terminally His-tagged enzyme, hanging drop vapour diffusion method, crystallization screening, mixing of 0.001 ml protein solution plus 0.001 ml reservoir solution containing 1.9 M ammonium sulfate, 100 mM Bis-Tris, pH 6.5, at 20°C, crystals are either soaked or cocrystallized with 5 mM NADP+ and with several moderate inhibitors that are identified from fragment library screening, crystal cryoprotection with reservoir solution containing 20% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 2.8-3.2 A resolution, modeling by molecular replacement using CaASADH, PDB ID 3hsk, as the search model
purified recombinant His6-tagged enzyme free or in complex with NADP+ and inhibitor 4-benzoquinone, hanging drop vapor diffusion, mixing of 12 mg/ml protein solution with reservoir solution containing 0.2 M ammonium citrate, pH 7.0, and 18% PEG 3350, for inhibitor complexed crystals soaking in reservoir solution with added 15% v/v ethylene glycol and 5 mM NADP+, X-ray diffraction structure determination and analysis at 2.4-2.6 A resolution, molecular replacement using the structure of Candida albicans ASADH (PDB ID 3hsk) as the search model
hanging drop vapor diffusion method, using 20% (w/v) PEG 400, 0.1 M HEPES pH 6.5, 0.1 M MgCl2, at 20°C
purified recombinant C-terminally His-tagged enzyme, hanging drop vapour diffusion method, crystallization screening, mixing of 9 mg/ml protein solution with reservoir solution containing 10% PEG 8000, 6% ethylene glycol, 0.1 M HEPES pH 7.5, in a 2:1 ration, at 20°C, crystals are cocrystallized with 4 mM NADP+, X-ray diffraction structure determination and analysis at 2.6 A resolution, modeling by molecular replacement
enzyme in open and closed form, 30 mg/ml purified recombinant enzyme in 10 mM Tris, pH 7.4, 40 mM KCl, with equal volume of reservoir solution, 0.006 ml sitting drops by vapour diffusion utilizing micro-bridges, 20% v/v ethylene glycol, 4°C, X-ray diffraction structure determination and analysis at 1.95 A and 1.6 A resolution, respectively, modeling
purified enzyme, X-ray diffractions structure determination and analysis at 2.45 A resolution
10 mg/ml purified recombinant wild-type and mutant enzymes free or in complex with the substrates, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, 1 mM DTT, by hanging drop vapour diffusion, 20°C, mixed with equal volume of precipitant solution containing 22-24% PEG 3350, and 0.2 M ammonium acetate, crystals are soaked for 1 h in a solution containing 2 mM aspartate-beta-semialdehyde or 100 mM phosphate, 26% PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris-HCl, pH 8.5, and 20% glycerol, X-ray diffraction structure determination and analysis at about 2.0 A resolution
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15 mg/ml purified recombinant enzyme, in 10 mM HEPES, pH 7.0, 1 mM EDTA, 1 mM DTT, crystallized as apoenzyme, as hemithioacetal, or as hemithioacetal structure with bound phosphate, hanging drop vapour diffusion method, 20°C, 1:1 mixture of protein solution and precipitant solution, the latter containing 24-28% PEG 3350, 0.2 M ammonium acetate, 0.1 M Tris, pH 8.5, overnight, substrate complexing by soaking of crystals in mother liquor with 50 mM potassium phosphate, crystals are frozen in precipitant solution with 20% glycerol added, X-ray diffraction structure determination and analysis at 2.0-2.15 A resolution, modeling
15 mg/ml purified recombinant wild-type enzyme in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, enzyme is free or complexed with substrates phosphate and/or asparate-beta-semialdehyde, hanging drop vapour diffusion method, 20°C, against an equal volume of precipitant solution containing 24-28% PEG 3350, 0.2 M ammonium acetate, and 0.1 M Tris-HCl, pH 8.5, soaking of crystals before harvest in 100 mM phosphate and 2 mM aspartate-beta-semialdehyde, crystallization of mutant H277N in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, by addition of precipitant solution containing 5 mM NADP+ and 5 mM inhibitor S-methyl-L-cysteine sulfoxide, 22% PEG 3350, 0.2 M ammonium acetate and 0.1 M sodium cacodylate, pH 6.5, X-ray diffraction structure determination and analysis at about 2.0 A resolution
about 10 mg/ml pure recombinant wild-type enzyme in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, complexed with oxyanions arsenate or periodate, hanging drop vapour diffusion method, 20°C, against an equal volume of precipitant solution containing 22-24% PEG 4000, 0.2 M ammonium acetate, and Tris-HCl, pH 8.5, soaking of crystals before harvest in a solution containing 26% PEG3350, 0.2 M ammonium acetate, 100 mM periodate or arsenate,0.1 M Tris-HCl, pH 8.5, and 20% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution
the structure of aspartate-beta-semialdehyde dehydrogenase has been determined to 2.3 A resolution using multiwavelength anomalous diffraction phasing of a seleno-methionine-substituted derivative
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by using the hanging-drop vapour-diffusion method, crystallization in 2 different crystal forms, diffraction data analysis suggests the presence of up to four monomers in the asymmetric unit of the orthorhombic crystal form and of one or 2 monomers in the cubic crystal form
in complex with S-methyl-l-cysteine sulfoxide and sulfate, sitting drop vapor diffusion method, using 1.6 M ammonium sulfate and 100 mM citric acid pH 5.0
purified recombinant His-tagged enzyme, 9 mg/ml protein in 10 mM potassium phosphate buffer, pH 8.0, and 10 mM DTT, sitting drop vapour diffusion method, mixing of 500 nl of protein and of reservoir solution, the latter containing 1.6 M ammonium sulfate and 100 mM citric acid, pH 5.0, 2 days at 18°C, two different crystal forms, X-ray diffraction structure determination and analysis at 2.18-2.75 A resolution
crystallization of the apo-enzyme, in complex with NADP+, in complex with L-aspartate-beta-semialdehyde, in complex with NADP+ and L-aspartate-beta-semialdehyde
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12 mg/ml purified recombinant enzyme free or in ternary complex with NADP+ and covalently bound inhibitor S-methyl-L-cysteine sulfoxide, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, hanging drop vapour diffusion method, 20°C, with or without 5 mM NADP+ and 5 mM inhibitor, against an equal volume of precipitant solution: containing 18% PEG 3350, 0.2 M sodium acetate, and 0.1 M Tris, pH 8.5 for the free enzyme, or containing 22% PEG 3350, 0.2 M sodium acetate, and 0.1 M sodium citrate, pH 5.6 for the ternary complex, addition of 20% glycerol for crystal freezing, X-ray diffraction structure determination and analysis at 2.8 A and 1.84 A resolution, respectively
apoenzyme and enzyme in complex with substrate L-aspartate semialdehyde, method optimization, purified protein in 50 mM sodium citrate, pH 5.6, with 0.2 M ammonium acetate and 2 mM DTT via dialysis overnight, hanging drop vapour diffusion method, 4°C, diluted back into 100 mM Tris, pH 8.5, with 200 mM ammonium acetate and 5 mM DTT with 12 mg/ml protein, 0.001 ml protein solution is mixed with 0.001 ml of precipitant containing 0.1 M sodium citrate, pH 5.5-6.5, 5 mM DTT, 0.1-0.4 M ammonium acetate, and 24-27% PEG 8000, method optimization, overview, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution, molecular replacement method
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