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Literature summary 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

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.11 overexpression Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.11 0.151
-
 L-Asp
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.11 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
4.1.1.11 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
4.1.1.11 59000
-
 gel filtration Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.11 recombinant enzyme Escherichia coli

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.1.1.11 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.11 0.57
-
 L-Asp
-
 Escherichia coli