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Literature summary extracted from

  • Spencer, P.; Jordan, P.M.
    Purification and characterization of 5-aminolevulinic acid dehydratase from Escherichia coli and a study of the reactive thiols at the metal-binding domain (1993), Biochem. J., 290, 279-287.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.2.1.24 0.8
-
 5-aminolevulinate at pH 6 and pH 8.5 Escherichia coli
4.2.1.24 1
-
 5-aminolevulinate at pH 6.8 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.2.1.24 Mg2+ can not activate the apoenzyme alone, but is able to substitute for the second molar equivalent of bound Zn2+ leading to a further 4fold stimulation Escherichia coli
4.2.1.24 Zn2+ required Escherichia coli
4.2.1.24 Zn2+ 2 mol of Zn2+ bound per mol of subunit Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.2.1.24 36000
-
 8 * 36000, SDS-PAGE Escherichia coli
4.2.1.24 270000
-
 gel filtration Escherichia coli

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
4.2.1.24
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.2.1.24 0.55
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.24 5-aminolevulinate + 5-aminolevulinate
-
 Escherichia coli porphobilinogen + 2 H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.24 octamer 8 * 36000, SDS-PAGE Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.2.1.24 8.5
-
-
 Escherichia coli