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Literature summary for 2.5.1.55 extracted from

  • Shulami, S.; Furdui, C.; Adir, N.; Shoham, Y.; Anderson, K.S.; Baasov, T.
    A reciprocal single mutation affects the metal requirement of 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) synthases from Aquifex pyrophilus and Escherichia coli (2004), J. Biol. Chem., 279, 45110-45120.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
EDTA
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
C11N enzyme retains 10% of the wild-type activity in absence of metal ions. Addition of divalent metal ions does not affect the catalytic activity of the mutant enzyme and the catalytic efficiency, i.e. the ratio of turnover number to Km-value, is reduced only 12fold, the mutant enzyme has become metal-independent Aquifex pyrophilus
N26C activity of the wild-type enzyme is independent of metal ions, the activity of mutant enzyme is decreased by EDTA and increased by Mn2+ and Cd2+ Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline inhibits wild-type enzyme, no inhibition of mutant enzyme C11N Aquifex pyrophilus
EDTA inhibits wild-type enzyme, no inhibition of mutant enzyme C11N Aquifex pyrophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0058
-
phosphoenolpyruvate pH 7.5, 37°C, Cd2+ mutant enzyme N26C Escherichia coli
0.006
-
phosphoenolpyruvate pH 7.5, 37°C, wild-type enzyme Escherichia coli
0.017
-
phosphoenolpyruvate pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated Aquifex pyrophilus
0.019
-
phosphoenolpyruvate pH 7.5, 37°C, Mn2+ mutant enzyme N26C Escherichia coli
0.02
-
D-arabinose 5-phosphate pH 7.5, 37°C, wild-type enzyme Escherichia coli
0.026
-
phosphoenolpyruvate pH 7.5, 60°C, wild-type Mn2+-enzyme Aquifex pyrophilus
0.032
-
phosphoenolpyruvate pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated Escherichia coli
0.067
-
D-arabinose 5-phosphate pH 7.5, 60°C, wild-type Mn2+-enzyme Aquifex pyrophilus
0.07
-
D-arabinose 5-phosphate pH 7.5, 37°C, Mn2+ mutant enzyme N26C Escherichia coli
0.075
-
D-arabinose 5-phosphate pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated Escherichia coli
0.11
-
D-arabinose 5-phosphate pH 7.5, 37°C, Cd2+ mutant enzyme N26C Escherichia coli
0.14
-
D-arabinose 5-phosphate pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated Aquifex pyrophilus

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ increase in steady-state rate of wild-type enzyme, Km: 0.0006 mM Aquifex pyrophilus
Iron wild-type enzyme contains 0.19 mol of iron per mol of enzyme, mutant enzyme c11N contains 0.22 mol of iron per mol of enzyme Aquifex pyrophilus
Magnesium wild-type enzyme contains 0.05 mol of magnesium per mol of enzyme, mutant enzyme N26C contains 0.4 mol of magnesium per mol of enzyme Escherichia coli
Mn2+ 200fold increase in steady-state rate of wild-type enzyme, Km: 0.01 mM. Addition of Mn2+ up to 2 mM does not stimulate the reaction rate of C11N mutant Aquifex pyrophilus
Zinc wild-type enzyme contains 0.05 mol of zinc per mol of enzyme, mutant enzyme N26C contains 0.2 mol of zinc per mol of enzyme Escherichia coli
Zinc wild-type enzyme contains 0.26 mol per mol of enzyme, mutant enzyme c11N contains 0.02 mol of zinc per mol of enzyme. Aquifex pyrophilus

Organism

Organism UniProt Comment Textmining
Aquifex pyrophilus Q8GLK7
-
-
Escherichia coli P0A715
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphoenolpyruvate + D-arabinose 5-phosphate
-
Escherichia coli 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
-
Aquifex pyrophilus 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
?

Synonyms

Synonyms Comment Organism
3-deoxy-D-manno-2-octulosonate-8-phosphate synthase
-
Escherichia coli
3-deoxy-D-manno-2-octulosonate-8-phosphate synthase
-
Aquifex pyrophilus
Kdo8P synthase
-
Escherichia coli
Kdo8P synthase
-
Aquifex pyrophilus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.36
-
phosphoenolpyruvate pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated Escherichia coli
0.36
-
D-arabinose 5-phosphate pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated Escherichia coli
0.42
-
phosphoenolpyruvate pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated Aquifex pyrophilus
0.42
-
D-arabinose 5-phosphate pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated Aquifex pyrophilus
1.9
-
phosphoenolpyruvate pH 7.5, 37°C, Cd2+ mutant enzyme N26C Escherichia coli
1.9
-
D-arabinose 5-phosphate pH 7.5, 37°C, Cd2+ mutant enzyme N26C Escherichia coli
1.9
-
phosphoenolpyruvate pH 7.5, 37°C, Mn2+ mutant enzyme N26C Escherichia coli
1.9
-
D-arabinose 5-phosphate pH 7.5, 37°C, Mn2+ mutant enzyme N26C Escherichia coli
6.1
-
phosphoenolpyruvate pH 7.5, 37°C, wild-type enzyme Escherichia coli
6.1
-
D-arabinose 5-phosphate pH 7.5, 37°C, wild-type enzyme Escherichia coli
9
-
phosphoenolpyruvate pH 7.5, 60°C, wild-type Mn2+-enzyme Aquifex pyrophilus
9
-
D-arabinose 5-phosphate pH 7.5, 60°C, wild-type Mn2+-enzyme Aquifex pyrophilus