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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.
    View publication on PubMedView publication on EuropePMC

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
a

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