Application | Comment | Organism |
---|---|---|
additional information | enzyme is an attractive target for development of antibacterial, fungicidal, or herbicidal compounds | 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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Vibrio cholerae | Q9KQG2 | El Tor N16961, TIGR locus VC2036 | - |
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 |
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 | Comment | Organism |
---|---|---|
dimer | crystal structure, communication mechanism between the active sites of the subunits, overview | Vibrio cholerae |
Synonyms | Comment | Organism |
---|---|---|
ASADH | - |
Vibrio cholerae |
aspartate-beta-semialdehyde dehydrogenase | - |
Vibrio cholerae |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | binding mechanism and structure | Vibrio cholerae | |
NADPH | - |
Vibrio cholerae |