5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase
This is an abbreviated version!
For detailed information about glutamate-1-semialdehyde 2,1-aminomutase, go to the full flat file.
Word Map on EC 5.4.3.8
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5.4.3.8
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chlorophyll
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5-aminolevulinic
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tetrapyrrole
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glutamyl-trna
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delta-aminolevulinic
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synechococcus
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gabaculine
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hema
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4,5-diaminovalerate
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trnaglu
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4,5-dioxovalerate
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aldimine
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glutr
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five-carbon
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glutamyl-trnaglu
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trna-dependent
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3-amino-2,3-dihydrobenzoic
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chelatase
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mg-chelatase
- 5.4.3.8
- chlorophyll
-
5-aminolevulinic
- tetrapyrrole
- glutamyl-trna
-
delta-aminolevulinic
- synechococcus
- gabaculine
- hema
- 4,5-diaminovalerate
- trnaglu
- 4,5-dioxovalerate
-
aldimine
- glutr
-
five-carbon
-
glutamyl-trnaglu
-
trna-dependent
-
3-amino-2,3-dihydrobenzoic
- chelatase
-
mg-chelatase
Reaction
Synonyms
Aminotransferase, glutamate semialdehyde, AtGSA1, EC 2.7.2.13, Glutamate 1-semialdehyde aminotransferase, glutamate-1-semialdehyde amino-transferase, glutamate-1-semialdehyde aminomutase, Glutamate-1-semialdehyde aminotransferase, glutamate-1-semialdehyde-2,1-aminomutase, glutamate-1-semialdehyde-aminomutase, GSA, GSA aminotransferase, GSA-AT, GSA1, GSAM, GSAT, HemL, PA4088, protein PA4088
ECTree
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Crystallization
Crystallization on EC 5.4.3.8 - glutamate-1-semialdehyde 2,1-aminomutase
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purified recombinant detagged enzyme, sitting drop vapour diffusion method, mixing of 0.001 ml of 8 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 200 mM NaCl, with 0.001 ml of reservoir solution containing 0.15 M potassium bromide, and 30% w/v PEG 2000 MME, and equilibration against 0.2 ml reservoir solution, X-ray diffraction structure determination and analysis at 1.25 A resolution
in complex with pyridoxamine 5'-phosphate, hanging drop vapor diffusion method, using 0.1 M Bicine pH 8.5, 30% (w/v) PEG 3350, at 23°C
purified recombinant His-tagged wild-type enzyme and enzyme mutant K286A in complex with pyridoxamine 5'-phosphate cofactor, mixing of 10 mg/ml protein in 20 mM Tris, 200 mM NaCl, pH 8.0, with an equal volume of reservoir solution consisting of 0.2M ammonium sulfate, 0.1 M Bis-Tris, pH 6.5, and 25% PEG 3350 for the wild-type enzyme, and of 0.1 M Tris, pH 8.5, and 25% PEG3350 for the mutant enzyme, 20°C, 1 week, X-ray diffraction structure determination and analysis at 1.44-1.57 A resolution
wild type enzyme and mutant enzyme M248I are crystallized by the vapor diffusion method, using 11.5% (w/v) PEG 8.000 and 150 mM magnesium acetate, pH 6.8