BRENDA - Enzyme Database show

Capture of an intermediate in the catalytic cycle of L-aspartate-beta-semialdehyde dehydrogenase

Blanco, J.; Moore, R.A.; Viola, R.E.; Proc. Natl. Acad. Sci. USA 100, 12613-12617 (2003)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
1.2.1.11
pharmacology
enzyme is a target for development of antibiotics
Haemophilus influenzae
Crystallization (Commentary)
EC Number
Crystallization
Organism
1.2.1.11
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
Haemophilus influenzae
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.11
S-methyl cysteine sulfoxide
inhibitor binding structure deduced from crystal structure
Haemophilus influenzae
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Haemophilus influenzae
P44801
-
-
1.2.1.11
no activity in Homo sapiens
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
catalytic mechanism, identification and structural characterization of the tetrahedral reaction intermediate, substrate binding structure
Haemophilus influenzae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-aspartate-4-semialdehyde + phosphate + NADP+
-
657153
Haemophilus influenzae
L-4-aspartyl phosphate + NADPH
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
dependent on
Haemophilus influenzae
Application (protein specific)
EC Number
Application
Commentary
Organism
1.2.1.11
pharmacology
enzyme is a target for development of antibiotics
Haemophilus influenzae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
dependent on
Haemophilus influenzae
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.2.1.11
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
Haemophilus influenzae
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.11
S-methyl cysteine sulfoxide
inhibitor binding structure deduced from crystal structure
Haemophilus influenzae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.2.1.11
L-aspartate-4-semialdehyde + phosphate + NADP+
-
657153
Haemophilus influenzae
L-4-aspartyl phosphate + NADPH
-
-
-
?