Literature summary for 1.2.1.11 extracted from

Viola, R.E.; Liu, X.; Ohren, J.F.; Faehnle, C.R.
The structure of a redundant enzyme: a second isoform of aspartate beta-semialdehyde dehydrogenase in Vibrio cholerae (2008), Acta Crystallogr. Sect. D, D64, 321-330.

Application

Application	Comment	Organism
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 serotype O1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Vibrio cholerae serotype O1

Crystallization (Commentary)

Crystallization (Comment)	Organism
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 serotype O1

Crystallization (Comment)

Organism

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 serotype O1

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-aspartate 4-semialdehyde + phosphate + NADP+	Vibrio cholerae serotype O1	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

Organism	UniProt	Comment	Textmining
Vibrio cholerae serotype O1	-	isozymes ASADH1 and ASADH2	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant enzyme from Escherichia coli to over 95% purity by anion exchange chromatography and gel filtration	Vibrio cholerae serotype O1

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-aspartate 4-semialdehyde + phosphate + NADP+	-	Vibrio cholerae serotype O1	L-4-aspartyl phosphate + NADPH + H+	-	?
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	Vibrio cholerae serotype O1	L-4-aspartyl phosphate + NADPH + H+	-	?

Subunits

Subunits	Comment	Organism
dimer	-	Vibrio cholerae serotype O1

Synonyms

Synonyms	Comment	Organism
ASADH	-	Vibrio cholerae serotype O1
aspartate beta-semialdehyde dehydrogenase	-	Vibrio cholerae serotype O1

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	-	-	Vibrio cholerae serotype O1

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Vibrio cholerae serotype O1