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Literature summary for 4.2.1.24 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]

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

Metals/Ions

Metals/Ions Comment Organism Structure
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
Zn2+ required Escherichia coli
Zn2+ 2 mol of Zn2+ bound per mol of subunit Escherichia coli

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Subunits

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
Escherichia coli