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Literature summary for 4.1.1.11 extracted from

  • Schmitzberger, F.; Kilkenny, M.L.; Lobley, C.M.C.; Webb, M.E.; Vinkovic, M.; Matak-Vinkovic, D.; Witty, M.; Chirgadze, D.Y.; Smith, A.G.; Abell, C.; Blundell, T.L.
    Structural constraints on protein self-processing in L-aspartate-alpha-decarboxylase (2003), EMBO J., 22, 6193-6204.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of an unprocessed native proenzyme and of the mutants G24S, S25A, S25C, S25T, H11A, Ala-24 and Ala-26 insertion mutants, hanging-drop vapour-diffusion method Escherichia coli

Protein Variants

Protein Variants Comment Organism
G24S study of the structure and processing activity Escherichia coli
H11A study of the structure and processing activity Escherichia coli
additional information inactive Ala-24 and Ala-26 insertion mutants, study of the structure and processing activity Escherichia coli
S25A inactive mutant, study of the structure and processing activity Escherichia coli
S25C study of the structure and processing activity Escherichia coli
S25T inactive mutant, study of the structure and processing activity Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14000
-
4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Escherichia coli major route of beta-alanine production essential for the biosynthesis of pantothenate beta-alanine + CO2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P0A790
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification ADC, which is translated as inactive pro-protein, i.e. pi-protein, undergoes intramolecular self-cleavage at Gly-24/Ser-25 producing the alpha- and beta-subunit, molecular mechanism of self-processing, slow process Escherichia coli

Purification (Commentary)

Purification (Comment) Organism
native pro-ADC and mutants Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-aspartate Thr-57 and a water molecule are probable catalytic residues able to support acid-base catalysis, enzyme structure Escherichia coli beta-alanine + CO2
-
?
L-aspartate major route of beta-alanine production essential for the biosynthesis of pantothenate Escherichia coli beta-alanine + CO2
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 14000, about, native pi-protein, secondary structure, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
ADC
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
additional information the translated inactive proenzyme, pi-enzyme, self-processes to create its own covalently bound prosthetic group, a pyruvoyl cofactor, mechanism Escherichia coli