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Literature summary extracted from

  • Sabo, D.L.; Boeker, E.A.; Byers, B.; Waron, H.; Fischer, E.H.
    Purification and physical properties of inducible Escherichia coli lysine decarboxylase (1974), Biochemistry, 13, 662-670.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.1.18
-
 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.18 NaCl 1 M, 45% inhibition Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.18 80000
-
 x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.18 L-Lys Escherichia coli inducible enzyme ?
-
 ?
4.1.1.18 L-Lys Escherichia coli B / ATCC 11303 inducible enzyme ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.18 Escherichia coli
-
-
-
4.1.1.18 Escherichia coli B / ATCC 11303
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.18
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.18 1018
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.18 delta-Hydroxylysine 25% of the activity with L-Lys Escherichia coli 1,5-Diamino-2-hydroxypentane + CO2
-
 ?
4.1.1.18 delta-Hydroxylysine 25% of the activity with L-Lys Escherichia coli B / ATCC 11303 1,5-Diamino-2-hydroxypentane + CO2
-
 ?
4.1.1.18 L-Lys
-
 Escherichia coli Cadaverine + CO2
-
 ?
4.1.1.18 L-Lys
-
 Escherichia coli B / ATCC 11303 Cadaverine + CO2
-
 ?
4.1.1.18 L-Lys inducible enzyme Escherichia coli ?
-
 ?
4.1.1.18 L-Lys inducible enzyme Escherichia coli B / ATCC 11303 ?
-
 ?
4.1.1.18 S-Aminoethyl-L-Cys 15% of the activity with L-Lys Escherichia coli 1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
-
 ?
4.1.1.18 S-Aminoethyl-L-Cys 15% of the activity with L-Lys Escherichia coli B / ATCC 11303 1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.18 ? x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.18 5.7
-
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.18 4.7 6.6 50% of maximal activity at pH 4.7 and 6.6 Escherichia coli