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Literature summary extracted from

  • Alvarez, E.; Ramon, F.; Magan, C.; Diez, E.
    L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme (2004), Biochim. Biophys. Acta, 1696, 23-29.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.11 D-Cystine 70% inhibition at 0.01 mM, binds via the cysteine moiety covalently to the catalytic Cys135 of the enzyme, pH-dependent proces, optimal at pH 7.0-7.5, inhibition is reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione, no protection by aspartate-beta-semialdehyde, NADP+ or NADPH, inhibition mechanism and kinetics Escherichia coli
1.2.1.11 DTNB reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione Escherichia coli
1.2.1.11 GSSG oxidized glutathione Escherichia coli
1.2.1.11 L-2-Amino-4-oxo-5-chloropentanoic acid substrate analogue, irreversible inactivation, pseudo-first-order kinetics Escherichia coli
1.2.1.11 L-cystine complete inhibition at 0.01 mM, binds via the cysteine moiety covalently to the catalytic Cys135 of the enzyme, pH-dependent process, optimal at pH 7.0-7.5, inhibition is reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione, no protection by aspartate-beta-semialdehyde, NADP+ or NADPH, inhibition mechanism and kinetics Escherichia coli
1.2.1.11 L-cystine diethyl ester 68% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione Escherichia coli
1.2.1.11 L-cystine dimethyl ester 67% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione Escherichia coli
1.2.1.11 L-cystine hydroxamate 20% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione Escherichia coli
1.2.1.11 additional information no inhibition by N,N'-diacetyl-L-cystine, L-cystine di-beta-naphthylamide, disulfiram, N-acetyl-L-cystine, 2,2-dithiodipyridine, 4,4-dithiodipyridine, L- and D-cysteine, and oxidized and reduced coenzyme A Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.11 Escherichia coli
-
-
-

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 Cys135 is essential for activity Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.1.11 L-aspartate-4-semialdehyde + phosphate + NADP+
-
 Escherichia coli L-4-aspartyl phosphate + NADPH reverse reaction: reductive dephosphorylation r

Synonyms

EC Number Synonyms Comment Organism
1.2.1.11 ASADH
-
 Escherichia coli
1.2.1.11 aspartate-beta-semialdehyde dehydrogenase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.2.1.11 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.2.1.11 7.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.11 NADP+
-
 Escherichia coli
1.2.1.11 NADPH
-
 Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.2.1.11 additional information
-
 additional information inhibition kinetics at 21°C and pH 7.5 Escherichia coli