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Literature summary for 4.1.1.11 extracted from

  • Ramjee, M.K.; Genschel, U.; Abell, C.; Smith, A.G.
    Escherichia coli L-aspartate alpha-decarboxylase: preprotein processing and observation of reaction intermediates by electrospray mass spectrometry (1997), Biochem. J., 323, 661-669.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Pyruvoyl group contains 3 pyruvoyl groups per tetrameric enzyme Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
overexpression Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.151
-
L-Asp
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
11000
-
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine Escherichia coli
13800
-
x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine Escherichia coli
59000
-
gel filtration Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Aspartate
-
Escherichia coli beta-Ala + CO2
-
?

Subunits

Subunits Comment Organism
tetramer x * 2800, beta, + x * 11000, alpha, + x * 13800, pi, SDS-PAGE, enzyme comprises principally the unprocessed pi-subunit, with a small proportion of the alpha-subunit and the beta-subunit. The enzyme is synthesized initially as an inactive proenzyme, the pi-protein, which is proteolytically cleaved at a specific X-Ser bond to produce a beta-subunit with XOH at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus, derived from serine Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.57
-
L-Asp
-
Escherichia coli