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Literature summary for 4.2.1.7 extracted from

  • Dreyer, J.L.
    The role of iron in the activation of mannonic and altronic acid hydratases, two Fe-requiring hydro-lyases (1987), Eur. J. Biochem., 166, 623-630.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
Escherichia coli
alpha-picolinate
-
Escherichia coli
EDTA
-
Escherichia coli
Fe2+ low concentrations required, inhibition above 2 mM Escherichia coli
iodoacetate
-
Escherichia coli
nitrilotriacetic acid
-
Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ low concentrations required, inhibition above 2 mM. Upon activation the enzyme incorporates a single Fe atom. The incorporated iron is losely bound. Synergistic activation in presence of both, Mg2+ and Mn2+ Escherichia coli
Mn2+ activates, synergistic activation in presence of both, Mg2+ and Mn2+. Mn2+ appears to be a constituent of the enzyme active center Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53000
-
x * 53000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-altronate
-
Escherichia coli 2-dehydro-3-deoxy-D-gluconate + H2O
-
?

Subunits

Subunits Comment Organism
? x * 53000, SDS-PAGE Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.6 about 20% of maximal activity at pH 6.5 and at pH 8.6 Escherichia coli