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Literature summary for 1.2.1.11 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

Inhibitors Comment Organism Structure
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
DTNB reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione Escherichia coli
GSSG oxidized glutathione Escherichia coli
L-2-Amino-4-oxo-5-chloropentanoic acid substrate analogue, irreversible inactivation, pseudo-first-order kinetics Escherichia coli
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
L-cystine diethyl ester 68% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione Escherichia coli
L-cystine dimethyl ester 67% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione Escherichia coli
L-cystine hydroxamate 20% inhibition at 0.01 mM, reversible by DTT, dithioerythritol, 2-mercaptoethanol, dimercaptopropanol, and reduced glutathione Escherichia coli
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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH + H+ catalytic Cys135 is essential for activity Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ASADH
-
Escherichia coli
aspartate-beta-semialdehyde dehydrogenase
-
Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NADP+
-
Escherichia coli
NADPH
-
Escherichia coli

Ki Value [mM]

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