Literature summary for 1.2.1.11 extracted from

Blanco, J.; Moore, R.A.; Kabaleeswaran, V.; Viola, R.E.
A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae (2003), Protein Sci., 12, 27-33.

Application

Application	Comment	Organism
additional information	enzyme is an attractive target for development of antibacterial, fungicidal, or herbicidal compounds	Vibrio cholerae

Crystallization (Commentary)

Crystallization (Comment)	Organism
12 mg/ml purified recombinant enzyme free or in ternary complex with NADP+ and covalently bound inhibitor S-methyl-L-cysteine sulfoxide, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, hanging drop vapour diffusion method, 20°C, with or without 5 mM NADP+ and 5 mM inhibitor, against an equal volume of precipitant solution: containing 18% PEG 3350, 0.2 M sodium acetate, and 0.1 M Tris, pH 8.5 for the free enzyme, or containing 22% PEG 3350, 0.2 M sodium acetate, and 0.1 M sodium citrate, pH 5.6 for the ternary complex, addition of 20% glycerol for crystal freezing, X-ray diffraction structure determination and analysis at 2.8 A and 1.84 A resolution, respectively	Vibrio cholerae

Crystallization (Comment)

Organism

12 mg/ml purified recombinant enzyme free or in ternary complex with NADP+ and covalently bound inhibitor S-methyl-L-cysteine sulfoxide, protein in 10 mM HEPES, pH 7.0, 1 mM EDTA, and 1 mM DTT, hanging drop vapour diffusion method, 20°C, with or without 5 mM NADP+ and 5 mM inhibitor, against an equal volume of precipitant solution: containing 18% PEG 3350, 0.2 M sodium acetate, and 0.1 M Tris, pH 8.5 for the free enzyme, or containing 22% PEG 3350, 0.2 M sodium acetate, and 0.1 M sodium citrate, pH 5.6 for the ternary complex, addition of 20% glycerol for crystal freezing, X-ray diffraction structure determination and analysis at 2.8 A and 1.84 A resolution, respectively

Vibrio cholerae

Inhibitors

Inhibitors	Comment	Organism	Structure
L-cystine	inactivation, reversible by addition of DTT or 2-mercaptoethanol	Vibrio cholerae
S-methyl-L-cysteine sulfoxide	covalently binding inhibitor via Cys134 at the active site, inactivation, inhibition and binding mechanism, reversible by addition of DTT or 2-mercaptoethanol	Vibrio cholerae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-4-aspartyl phosphate + NADPH	Vibrio cholerae	reductive dephosphorylation in the aspartate biosynthetic pathway of plants and microorganisms	L-aspartate-4-semialdehyde + phosphate + NADP+	-	r

Organism

Organism	UniProt	Comment	Textmining
Vibrio cholerae	Q9KQG2	El Tor N16961, TIGR locus VC2036	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+	catalytic mechanism, active site structure, catalytic nucleophile is Cys134	Vibrio cholerae	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-4-aspartyl phosphate + NADPH	reductive dephosphorylation in the aspartate biosynthetic pathway of plants and microorganisms	Vibrio cholerae	L-aspartate-4-semialdehyde + phosphate + NADP+	-	r
L-aspartate-4-semialdehyde + phosphate + NADP+	-	Vibrio cholerae	L-4-aspartyl phosphate + NADPH	reverse reaction: reductive dephosphorylation	r

Subunits

Subunits	Comment	Organism
dimer	crystal structure, communication mechanism between the active sites of the subunits, overview	Vibrio cholerae

Synonyms

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

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	binding mechanism and structure	Vibrio cholerae
NADPH	-	Vibrio cholerae