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The structure of a redundant enzyme: a second isoform of aspartate beta-semialdehyde dehydrogenase in Vibrio cholerae

Viola, R.E.; Liu, X.; Ohren, J.F.; Faehnle, C.R.; Acta Crystallogr. Sect. D D64, 321-330 (2008)

Data extracted from this reference:

Application
EC Number
Application
Commentary
Organism
1.2.1.11
drug development
ASADH is a target for the development of novel antibiotics, especially for Gram-negative bacteria that require diaminopimelate for cell-wall biosynthesis
Vibrio cholerae
Cloned(Commentary)
EC Number
Commentary
Organism
1.2.1.11
expression in Escherichia coli
Vibrio cholerae
Crystallization (Commentary)
EC Number
Crystallization
Organism
1.2.1.11
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
Vibrio cholerae
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-aspartate 4-semialdehyde + phosphate + NADP+
Vibrio cholerae
the essential ASADH produces the first branch-point metabolite in the biosynthetic pathways that lead to the production of lysine, threonine, methionine and isoleucine as well as the cell-wall precursor diaminopimelate
L-4-aspartyl phosphate + NADPH + H+
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.2.1.11
Vibrio cholerae
-
isozymes ASADH1 and ASADH2
-
Purification (Commentary)
EC Number
Commentary
Organism
1.2.1.11
recombinant enzyme from Escherichia coli to over 95% purity by anion exchange chromatography and gel filtration
Vibrio cholerae
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+
-
684158
Vibrio cholerae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
the essential ASADH produces the first branch-point metabolite in the biosynthetic pathways that lead to the production of lysine, threonine, methionine and isoleucine as well as the cell-wall precursor diaminopimelate
684158
Vibrio cholerae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.2.1.11
dimer
-
Vibrio cholerae
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.1.11
8.5
-
-
Vibrio cholerae
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Vibrio cholerae
Application (protein specific)
EC Number
Application
Commentary
Organism
1.2.1.11
drug development
ASADH is a target for the development of novel antibiotics, especially for Gram-negative bacteria that require diaminopimelate for cell-wall biosynthesis
Vibrio cholerae
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.11
expression in Escherichia coli
Vibrio cholerae
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.2.1.11
NADP+
-
Vibrio cholerae
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.2.1.11
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
Vibrio cholerae
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-aspartate 4-semialdehyde + phosphate + NADP+
Vibrio cholerae
the essential ASADH produces the first branch-point metabolite in the biosynthetic pathways that lead to the production of lysine, threonine, methionine and isoleucine as well as the cell-wall precursor diaminopimelate
L-4-aspartyl phosphate + NADPH + H+
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.2.1.11
recombinant enzyme from Escherichia coli to over 95% purity by anion exchange chromatography and gel filtration
Vibrio cholerae
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+
-
684158
Vibrio cholerae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
1.2.1.11
L-aspartate 4-semialdehyde + phosphate + NADP+
the essential ASADH produces the first branch-point metabolite in the biosynthetic pathways that lead to the production of lysine, threonine, methionine and isoleucine as well as the cell-wall precursor diaminopimelate
684158
Vibrio cholerae
L-4-aspartyl phosphate + NADPH + H+
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.2.1.11
dimer
-
Vibrio cholerae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
1.2.1.11
8.5
-
-
Vibrio cholerae