Literature summary 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
EC Number |
Application |
Comment |
Organism |
---|
1.2.1.11 |
additional information |
enzyme is an attractive target for development of antibacterial, fungicidal, or herbicidal compounds |
Vibrio cholerae |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
1.2.1.11 |
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
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.2.1.11 |
L-cystine |
inactivation, reversible by addition of DTT or 2-mercaptoethanol |
Vibrio cholerae |
|
1.2.1.11 |
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)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
1.2.1.11 |
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
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.2.1.11 |
Vibrio cholerae |
Q9KQG2 |
El Tor N16961, TIGR locus VC2036 |
- |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
1.2.1.11 |
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+ |
catalytic mechanism, active site structure, catalytic nucleophile is Cys134 |
Vibrio cholerae |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.2.1.11 |
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 |
|
1.2.1.11 |
L-aspartate-4-semialdehyde + phosphate + NADP+ |
- |
Vibrio cholerae |
L-4-aspartyl phosphate + NADPH |
reverse reaction: reductive dephosphorylation |
r |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.2.1.11 |
dimer |
crystal structure, communication mechanism between the active sites of the subunits, overview |
Vibrio cholerae |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.2.1.11 |
ASADH |
- |
Vibrio cholerae |
1.2.1.11 |
aspartate-beta-semialdehyde dehydrogenase |
- |
Vibrio cholerae |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.2.1.11 |
NADP+ |
binding mechanism and structure |
Vibrio cholerae |
|
1.2.1.11 |
NADPH |
- |
Vibrio cholerae |
|