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Structural basis for discrimination between oxyanion substrates or inhibitors in aspartate-beta-semialdehyde dehydrogenase

Faehnle, C.R.; Blanco, J.; Viola, R.E.; Acta Crystallogr. Sect. D 60, 2320-2324 (2004)

Data extracted from this reference:

Crystallization (Commentary)
EC Number
Crystallization
Organism
1.2.1.11
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
Haemophilus influenzae
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.11
additional information
inhibitor binding structure and mechanism
Haemophilus influenzae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH
Haemophilus influenzae
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
L-aspartate-4-semialdehyde + phosphate + NADP+
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Haemophilus influenzae
P44801
gene asd
-
Reaction
EC Number
Reaction
Commentary
Organism
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+
catalytic mechanism, substrate recognition
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-4-aspartyl phosphate + NADPH
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
654112
Haemophilus influenzae
L-aspartate-4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-aspartate-4-semialdehyde + phosphate + NADP+
formation of an acyl-enzyme intermediate
654112
Haemophilus influenzae
L-4-aspartyl phosphate + NADPH
-
-
-
r
1.2.1.11
additional information
oxyanion binding sites and structures with arsenate and periodate
654112
Haemophilus influenzae
?
-
-
-
-
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Haemophilus influenzae
1.2.1.11
NADPH
-
Haemophilus influenzae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Haemophilus influenzae
1.2.1.11
NADPH
-
Haemophilus influenzae
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.2.1.11
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
Haemophilus influenzae
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.2.1.11
additional information
inhibitor binding structure and mechanism
Haemophilus influenzae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1.2.1.11
L-4-aspartyl phosphate + NADPH
Haemophilus influenzae
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
L-aspartate-4-semialdehyde + phosphate + NADP+
-
-
r
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-4-aspartyl phosphate + NADPH
physiological forward reaction, reductive dephosphorylation in the aspartate biosynthetic pathway
654112
Haemophilus influenzae
L-aspartate-4-semialdehyde + phosphate + NADP+
-
-
-
r
1.2.1.11
L-aspartate-4-semialdehyde + phosphate + NADP+
formation of an acyl-enzyme intermediate
654112
Haemophilus influenzae
L-4-aspartyl phosphate + NADPH
-
-
-
r
1.2.1.11
additional information
oxyanion binding sites and structures with arsenate and periodate
654112
Haemophilus influenzae
?
-
-
-
-