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phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
? + phosphate
phosphoenolpyruvate + 2-deoxyribose 5-phosphate
?
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
phosphoenolpyruvate + L-xylose 5-phosphate + H2O
?
-
-
-
?
phosphoenolpyruvate + ribose 5-phosphate
?
additional information
?
-
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
? + phosphate
-
-
-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
? + phosphate
-
2-deoxy-D-ribose 5-phosphate is a poor substrate
-
-
?
phosphoenolpyruvate + 2-deoxy-D-ribose 5-phosphate
? + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
specific for D-arabinose 5-phosphate
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
His185 is necessary for the correct binding of phosphoenolpyruvate and of a catalytic water molecule
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
ir
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
ir
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
irreversible reaction
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
Gram-negative bacteria
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
absolute specificity for phosphoenolpyruvate and D-arabinose-5-phosphate
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
irreversible reaction
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose 5-phosphate + H2O
3-deoxy-D-manno-octulosonate 8-phosphate + phosphate
-
-
-
-
?
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
the enzyme catalyzes the first commited step in the production of 2-dehydro-3-deoxy-D-octonate, an integral part of the inner core region of the lipopolysaccharide layer in Gram-negative bacteria
-
-
?
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
key enzyme in the lipopolysaccharide biosynthesis of gram-negative bacteria
-
-
?
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
2-dehydro-3-deoxy-D-octonate 8-phosphate is the phosphorylated precursor of 3-deoxy-D-manno-octulosonate, an essential sugar of the liposaccharide of gram-negative bacteria
-
-
?
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor
-
-
?
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
-
the enzyme is involved in KDO biosynthesis before its incorporation into the lipid A precursor
-
-
?
phosphoenolpyruvate + D-arabinose-5-phosphate + H2O
2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate
Gram-negative bacteria
-
second step in the biosynthesis of 3-deoxy-D-manno-2-octulosonic acid
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
-
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
-
the enzyme does not catalyze the condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-ribo-heptulosonate 7-phosphate
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
-
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
-
the enzyme does not catalyze the condensation of D-erythrose 4-phosphate and phosphoenolpyruvate to form 3-deoxy-D-ribo-heptulosonate 7-phosphate
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
-
24% of the activity with D-arabinose 5-phosphate
-
-
?
phosphoenolpyruvate + erythrose 4-phosphate
3-deoxy-D-ribo-heptulosonate 7-phosphate
-
-
-
-
?
phosphoenolpyruvate + ribose 5-phosphate
?
-
-
-
-
?
phosphoenolpyruvate + ribose 5-phosphate
?
-
7% of the activity with D-arabinose 5-phosphate
-
-
?
phosphoenolpyruvate + ribose 5-phosphate
?
-
-
-
-
?
additional information
?
-
-
D-glucose 6-phosphate and D-erythrose 4-phosphate are no substrates
-
-
?
additional information
?
-
-
the kinetic mechanism is sequential ordered ter ter, with Mn2+ binding first
-
-
-
additional information
?
-
-
in presence of D-erythrose 4-phosphate or D-ribose 5-phosphate the enzyme catalyzes the rapid consumption of approximately 1 mol of phosphoenolpyruvate per active site, after which consumption of phosphoenolpyruvate slows to a negligible but measurable rate
-
-
?
additional information
?
-
-
development of a one-pot enzyme essay for 3-deoxy-D-manno-octulosonate 8-phosphate synthesis, the reaction process involves the isomerization of D-ribulose 5-phosphate to D-arabinose 5-phosphate catalyzed by D-arabinose 5-phosphate isomerase (KdsD), the aldol condensation of D-arabinose 5-phosphate and phosphoenolpyruvate (PEP) catalyzed by KDO 8-phosphate synthetase (KdsA), and the hydrolysis of KDO-8-phosphate catalyzed by KDO 8-phosphate phosphatase (KdsC), the poduct is transferred to lipid A by KDO transferase from Escherichia coli (WaaA), method, overview
-
-
?
additional information
?
-
D-ribose 5-phosphate, D-lyxose 5-phosphate, and D-xylose 5-phosphate with altered configuration at C2, C3 or both C2 and C3 relative to D-arabinose 5-phosphate are no substrates for KDO8P synthase
-
-
?
additional information
?
-
-
D-ribose 5-phosphate, D-lyxose 5-phosphate, and D-xylose 5-phosphate with altered configuration at C2, C3 or both C2 and C3 relative to D-arabinose 5-phosphate are no substrates for KDO8P synthase
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Fe3+
-
1 mM, 5-10% stimulation
Li+
-
1 mM, 5-10% stimulation
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
Sr2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Ba2+
-
1 mM, 5-10% stimulation
Ba2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cd2+
-
presence of Cd2+ restores activity to metal-free enzyme, Cd2+ significantly enhances the stability of the enzyme and raises the Tm by 14°C
Cd2+
-
in the presence of the metal, the enzyme is asymmetric and appears to alternate catalysis between the active sites located on the other face. In the absence of metal, the asymmetry is lost
Cd2+
the enzyme is most active when the endogenous metal is removed by incubation with EDTA and replaced with Cd2+
Cd2+
-
maximal activation below 0.1 mM
Cd2+
second in enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
Cd2+
increase in steady-state rate of wild-type enzyme, Km: 0.0006 mM
Cd2+
-
stimulates sild-type enzyme above 0.4 mM, stimulation of mutant enzyme C11A above 1 mM
Cd2+
-
the Zn2+ in the enzyme can be quantitatively replaced by Cd2+ which increases the observed turnover number and decreases the apparent Km-value for D-arabinose-5-phosphate by 6.5fold
Cd2+
-
4 Cd2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer, Cd2+ reconstituted enzyme is less stable than that of Zn2+, Co2+ and Cu2+ enzymes
Cd2+
activates, stabilizes, active site bound by Cys18, His204, Glu241, and Asp252
Cd2+
activation of metal-dependent mutants, inhibition of wild type and metal-independent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cd2+
-
destabilizes the enzyme, overview
Co2+
-
presence of Co2+ restores activity to metal-free enzyme
Co2+
-
stimulates wild-type enzyme above 0.4 mM, no stimulation of mutant enzyme C11A
Co2+
-
full reactivation of EDTA-treated enzyme
Co2+
-
monomer and dimer are each bound with 1 metal ion, tetramer with 2
Co2+
no activation of wild type enzyme, adverse effect on mutant N23C, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Cu2+
-
maximal activation below 0.1 mM
Cu2+
third in enzyme activity, octahedral or distorted tetrahedral delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization, product is bound in its linear conformation in the crystal structure of the enzyme with Cu2+, greenish color of enzyme, new absorption peak at 380 nm instead of 505 nm
Cu2+
-
inhibits at high concentrations, stimulates below 0.001 mM
Cu2+
-
4 Cu2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer
Cu2+
no activation of mutant enzymes containing the N23C substitution, slight reduction of wild type enzyme activity, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Fe2+
wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations. Mutation H185G decreases the ability of the enzyme to bind Fe2+, but not Zn2+. Maximal activity, about 8-10% of the wild-type activity is obtained when the native metal is replaced with Cd2+
Fe2+
-
contains 0.2-0.3 equivalents of iron per enzyme subunit. FeSO4 stimulates
Fe2+
unsubstituted enzyme with lowest enzyme activity
Fe2+
no activation of wild type enzyme and metal-independent mutants, activation of N23C/D247E, N23C/C246S/D247E, inhibitory for N23C, N23C/C246S/P249A, N23C/C246S/D247E/P249A, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Iron
-
enzyme contains 0.19 mol of iron per mol of subunit
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
Mg2+
-
1 mM, 5-10% stimulation
Mg2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Mn2+
-
presence of Mn2+ restores activity to metal-free enzyme
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
Mn2+
-
stimulates wild-type enzyme above 0.4 mM, no stimulation of mutant enzyme C11A
Mn2+
-
full reactivation of EDTA-treated enzyme, Km value 0.130 mM
Mn2+
-
1 mM, 5-10% stimulation
Mn2+
no activation of wild type enzyme, activation of metal-dependent mutants, 15% reduced activity above 200 microM for mutant N23C/D247E/P249A, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Ni2+
-
full reactivation of EDTA-treated enzyme
Ni2+
no activation of wild type enzyme and metal-dependent mutants, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
Zinc
-
enzyme contains 0.26 mol of zinc per mol of subunit
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.
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
Zn2+
-
enzyme contains approximately 0.4 equivalents of zinc per enzyme subunit. Maximal activation below 0.1 mM Zn2+
Zn2+
wild-type enzyme contains Zn2+ and Fe2+ with the ratio Zn2+/Fe2+ ranging from 1 to 2 in different preparations
Zn2+
highest enzyme activity, square pyramidal delocalized electronic structure computed with quantum mechanics/molecular mechanics geometry optimization
Zn2+
-
the enzyme contains one mol of Zn per monomer, apoenzyme is catalytically inactive
Zn2+
-
4 Zn2+ are bound in native tetrameric enzyme, 2 in dimer, 1 in monomer
Zn2+
activates, stabilizes, active site bound
Zn2+
no activation of wild type enzyme, inhibitory for all cloned enzymes, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4
additional information
-
divalent metal ion required, with Mn2+, Co2+ and Cd2+ in decreasing order being able to restore activity to metal-free enzyme
additional information
the type of metal bound in the active site affects the behavior of the enzyme in vivo and the rate of product release in the crystal environment
additional information
-
the type of metal bound in the active site affects the behavior of the enzyme in vivo and the rate of product release in the crystal environment
additional information
-
non-metallo enzyme, no metal requirement
additional information
-
reactivation of EDTA-treated enzyme, in decreasing order: Mn2+ = Co2+ = Ni2+ = Fe2+ > Ca2+ = Mg2+ = Cd2+ > Zn2+ > Cu2+
additional information
-
no metal requirement
additional information
-
no metal requirement
additional information
-
divalent metal ions play an important role in the quaternary structure of the protein
additional information
the enzyme is specifically coordinated with Cd2+ or Zn2+ ions, and isothermal titration calorimetry and differential scanning fluorimetry reveal that Cd2+ thermally stabilizes the protein structure more efficiently than Zn2
additional information
-
the enzyme is specifically coordinated with Cd2+ or Zn2+ ions, and isothermal titration calorimetry and differential scanning fluorimetry reveal that Cd2+ thermally stabilizes the protein structure more efficiently than Zn2
additional information
-
no metal requirement
additional information
the metal chelator EDTA has no effect on the activity of the metal-independent wild type enzyme and on the metal-independent mutants C246S, D247E, D247E/P249A or P249A
additional information
-
the metal chelator EDTA has no effect on the activity of the metal-independent wild type enzyme and on the metal-independent mutants C246S, D247E, D247E/P249A or P249A
additional information
-
metal-independent enzyme. Mn2+ or Co2+ have no effect on enzyme stability
additional information
-
no stimulation by divalent cations
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.23 - 5
2-deoxy-D-ribose 5-phosphate
0.05
2-deoxyribose 5-phosphate
-
pH 7.6, 37°C
0.0005 - 3.7
D-arabinose 5-phosphate
0.057
L-xylose 5-phosphate
at 30°C
0.0000066 - 1.65
phosphoenolpyruvate
additional information
additional information
-
0.23
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.432
2-deoxy-D-ribose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
1.5
2-deoxy-D-ribose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
5
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.0005
D-arabinose 5-phosphate
same enzyme preparation as following, substitution with 50 microM Zn2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.00123
D-arabinose 5-phosphate
recombinant enzyme produced in Escherichia coli, native Zn2+ and Fe2+ not substituted, 100 mM Tris-acetate, pH 7.5, 40°C
0.00156
D-arabinose 5-phosphate
same enzyme preparation as following, substitution with 5 microM Cu2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.002
D-arabinose 5-phosphate
same enzyme preparation as following, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.00227
D-arabinose 5-phosphate
independently prepared enzyme, substitution with 50 microM Cd2+, pH 5.0, 40°C
0.0025
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.00318
D-arabinose 5-phosphate
independently prepared enzyme, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.0038
D-arabinose 5-phosphate
-
37°C
0.0044
D-arabinose 5-phosphate
-
pH 7.4, 25°C, wild-type enzyme
0.0057
D-arabinose 5-phosphate
wild type, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.00593
D-arabinose 5-phosphate
-
pH 6.5, 25°C, Cd2+-enzyme
0.00773
D-arabinose 5-phosphate
-
pH 6.5, 25°C
0.0079
D-arabinose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.008
D-arabinose 5-phosphate
-
pH 7.5, 60°C
0.0085
D-arabinose 5-phosphate
-
pH 7.4, 37°C
0.0093
D-arabinose 5-phosphate
-
pH 7.4, 37°C, wild-type enzyme
0.012
D-arabinose 5-phosphate
at 30°C
0.012
D-arabinose 5-phosphate
N23C mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.012
D-arabinose 5-phosphate
P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.012
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication
0.012
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.013
D-arabinose 5-phosphate
N23C/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.014
D-arabinose 5-phosphate
-
pH 7.4, 25°C, mutant enzyme P145S
0.015
D-arabinose 5-phosphate
-
pH 7.5, 70°C
0.019
D-arabinose 5-phosphate
-
pH 7.6, 37°C
0.01926
D-arabinose 5-phosphate
same enzyme preparation as before, substitution with 5 microM Cu2+, pH 5.0, 40°C
0.02
D-arabinose 5-phosphate
-
-
0.02
D-arabinose 5-phosphate
-
pH 7.3, 37°C
0.02
D-arabinose 5-phosphate
pH 7.5, 37°C, wild-type enzyme
0.021
D-arabinose 5-phosphate
-
37°C, pH 7.5
0.021
D-arabinose 5-phosphate
-
wild-type, pH 7.2, 37°C
0.022
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.024
D-arabinose 5-phosphate
-
mutant P245A, pH 7.2, 37°C
0.026
D-arabinose 5-phosphate
-
pH 7.3, 37°C
0.027
D-arabinose 5-phosphate
-
pH 7.5, 80°C
0.0385
D-arabinose 5-phosphate
-
pH 6.5, 25°C, Zn2+-enzyme
0.043
D-arabinose 5-phosphate
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
0.06
D-arabinose 5-phosphate
D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.06
D-arabinose 5-phosphate
N23C mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.067
D-arabinose 5-phosphate
pH 7.5, 60°C, wild-type Mn2+-enzyme
0.07
D-arabinose 5-phosphate
-
60°C, pH 7.0, 0.48 mM Cd2+
0.07
D-arabinose 5-phosphate
pH 7.5, 37°C, Mn2+ mutant enzyme N26C
0.074
D-arabinose 5-phosphate
-
pH 7.5, 90°C
0.074
D-arabinose 5-phosphate
D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.075
D-arabinose 5-phosphate
pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated
0.081
D-arabinose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.097
D-arabinose 5-phosphate
N23C/C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.107
D-arabinose 5-phosphate
N23C/C247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.109
D-arabinose 5-phosphate
N23C/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.11
D-arabinose 5-phosphate
pH 7.5, 37°C, Cd2+ mutant enzyme N26C
0.14
D-arabinose 5-phosphate
pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated
0.14
D-arabinose 5-phosphate
N23C/C247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.19
D-arabinose 5-phosphate
N23C/C246S/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.2
D-arabinose 5-phosphate
-
28°C, parent strain PR122
0.213
D-arabinose 5-phosphate
C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.22
D-arabinose 5-phosphate
-
37°C, parent strain PR122
0.23
D-arabinose 5-phosphate
-
37°C, mutant strain PR32
0.24
D-arabinose 5-phosphate
N23C/C247E mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.28
D-arabinose 5-phosphate
-
pH 7.4, 37°C, mutant enzyme P145S
0.285
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R
0.33
D-arabinose 5-phosphate
N23C/C247E/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.45
D-arabinose 5-phosphate
-
42°C, mutant strain PR32
0.498
D-arabinose 5-phosphate
N23C/C246S/D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.503
D-arabinose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.54
D-arabinose 5-phosphate
N23C/C246S/D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.594
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F139A
0.816
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, R117K
0.83
D-arabinose 5-phosphate
-
42°C, parent strain PR122
0.873
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114A
1.04
D-arabinose 5-phosphate
N23C/C246S mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1.1
D-arabinose 5-phosphate
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
2.63
D-arabinose 5-phosphate
-
mutant D243E, pH 7.2, 37°C
2.742
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R/R117Q
3.21
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, R117Q
3.6
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, F114R/R117Q/F139G
3.7
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R/R117A
0.0000066
phosphoenolpyruvate
same enzyme preparation as before, substitution with 5 microM Cu2+, pH 5.0, 40°C
0.00004
phosphoenolpyruvate
independently prepared enzyme, substitution with 50 microM Cd2+, pH 5.0, 40°C
0.00014
phosphoenolpyruvate
same enzyme preparation as following, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.00015
phosphoenolpyruvate
same enzyme preparation as following, substitution with 5 microM Cu2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.00016
phosphoenolpyruvate
independently prepared enzyme, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.00016
phosphoenolpyruvate
recombinant enzyme produced in Escherichia coli, native Zn2+ and Fe2+ not substituted, 100 mM Tris-acetate, pH 7.5, 40°C
0.00028
phosphoenolpyruvate
same enzyme preparation as following, substitution with 50 microM Zn2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.001
phosphoenolpyruvate
Km less than 0.001 mM, in the presence of D-arabinose 5-phosphate, at 30°C
0.0024
phosphoenolpyruvate
N23C/C247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0025
phosphoenolpyruvate
in the presence of L-xylose 5-phosphate, at 30°C
0.0025
phosphoenolpyruvate
-
pH and temperature not specified in the publication
0.0025
phosphoenolpyruvate
wild type, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0026
phosphoenolpyruvate
-
pH 7.8, Zn2+-reconstituted enzyme
0.0027
phosphoenolpyruvate
N23C/C247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0028
phosphoenolpyruvate
-
pH 7.4, 25°C, wild-type enzyme
0.0028
phosphoenolpyruvate
N23C mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0029
phosphoenolpyruvate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.0031
phosphoenolpyruvate
-
pH 7.4, 37°C
0.0033
phosphoenolpyruvate
N23C/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0036
phosphoenolpyruvate
-
37°C
0.0038
phosphoenolpyruvate
N23C/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0042
phosphoenolpyruvate
-
pH 7.4, 37°C, wild-type enzyme
0.00443
phosphoenolpyruvate
-
pH 6.5, 25°C
0.0047
phosphoenolpyruvate
P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0049
phosphoenolpyruvate
D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0052
phosphoenolpyruvate
-
mutant P245A, pH 7.2, 37°C
0.0053
phosphoenolpyruvate
-
pH 7.8, Cd2+-reconstituted enzyme
0.0054
phosphoenolpyruvate
N23C mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0058
phosphoenolpyruvate
pH 7.5, 37°C, Cd2+ mutant enzyme N26C
0.0058
phosphoenolpyruvate
-
pH 7.8, Cu2+-reconstituted enzyme
0.006
phosphoenolpyruvate
-
-
0.006
phosphoenolpyruvate
-
pH 7.3, 37°C
0.006
phosphoenolpyruvate
pH 7.5, 37°C, wild-type enzyme
0.00648
phosphoenolpyruvate
-
pH 6.5, 25°C, Cd2+-enzyme
0.0066
phosphoenolpyruvate
N23C/C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.0075
phosphoenolpyruvate
-
pH 6.5, 25°C, Zn2+-enzyme
0.0075
phosphoenolpyruvate
-
pH 7.8, Co2+-reconstituted enzyme
0.0077
phosphoenolpyruvate
N23C/C247E mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0085
phosphoenolpyruvate
D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0093
phosphoenolpyruvate
C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.0095
phosphoenolpyruvate
N23C/C246S/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.012
phosphoenolpyruvate
-
wild-type, pH 7.2, 37°C
0.012
phosphoenolpyruvate
-
wild-type, pH 7.5, temperature not specified in the publication
0.013
phosphoenolpyruvate
-
mutant D243E, pH 7.2, 37°C
0.014
phosphoenolpyruvate
-
pH and temperature not specified in the publication, mutant F139A
0.0153
phosphoenolpyruvate
N23C/C246S/D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.017
phosphoenolpyruvate
pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated
0.017
phosphoenolpyruvate
N23C/C247E/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.019
phosphoenolpyruvate
pH 7.5, 37°C, Mn2+ mutant enzyme N26C
0.022
phosphoenolpyruvate
N23C/C246S/D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.022
phosphoenolpyruvate
-
pH and temperature not specified in the publication, R117K
0.026
phosphoenolpyruvate
pH 7.5, 60°C, wild-type Mn2+-enzyme
0.028
phosphoenolpyruvate
-
pH 7.5, at 90°C
0.032
phosphoenolpyruvate
pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated
0.038
phosphoenolpyruvate
-
pH 7.5, at 80°C
0.043
phosphoenolpyruvate
-
pH 7.5, at 60°C or 70°C
0.05
phosphoenolpyruvate
N23C/C246S mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.058
phosphoenolpyruvate
-
pH and temperature not specified in the publication, mutant F114A
0.095
phosphoenolpyruvate
-
pH and temperature not specified in the publication, mutant F114R
0.26
phosphoenolpyruvate
-
pH 7.4, 25°C, mutant enzyme P145S
0.29
phosphoenolpyruvate
-
60°C, pH 7.0, 0.48 mM Cd2+
0.65
phosphoenolpyruvate
-
37°C, pH 7.5
1.65
phosphoenolpyruvate
-
pH 7.4, 37°C, mutant enzyme P145S
additional information
additional information
-
-
-
additional information
additional information
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
N23C/C246S/D247E mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/D247E mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
N23C/C246S/D247E/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/D247E/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
N23C/C246S/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.007 - 0.66
2-deoxy-D-ribose 5-phosphate
0.12
2-deoxyribose 5-phosphate
-
pH 7.6, 37°C
0.01 - 9
D-arabinose 5-phosphate
1.1
L-xylose 5-phosphate
at 30°C
0.02 - 100
phosphoenolpyruvate
additional information
additional information
-
0.007
2-deoxy-D-ribose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.13
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.202
2-deoxy-D-ribose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.66
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.01
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, R117A
0.108
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R/R117A
0.14
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, F114R/R117Q/F139G
0.149
D-arabinose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.178
D-arabinose 5-phosphate
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
0.27
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R/R117Q
0.3
D-arabinose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.32
D-arabinose 5-phosphate
mutant enzyme R1096G
0.333
D-arabinose 5-phosphate
-
0.36
D-arabinose 5-phosphate
pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated
0.38
D-arabinose 5-phosphate
-
pH 7.5, 60°C
0.42
D-arabinose 5-phosphate
pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated
0.48
D-arabinose 5-phosphate
wild-type enzyme
0.49
D-arabinose 5-phosphate
-
pH 6.5, 25°C, Zn2+-enzyme
0.74
D-arabinose 5-phosphate
-
pH 7.4, 25°C, mutant enzyme P145S
0.87
D-arabinose 5-phosphate
-
pH 7.5, 70°C
1
D-arabinose 5-phosphate
-
pH 7.4, 37°C
1.06
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, R117Q
1.08
D-arabinose 5-phosphate
-
pH 6.5, 25°C, Cd2+-enzyme
1.47
D-arabinose 5-phosphate
-
pH 7.5, 80°C
1.63
D-arabinose 5-phosphate
-
pH 7.4, 37°C, mutant enzyme P145S
1.75
D-arabinose 5-phosphate
-
pH 7.4, 25°C, wild-type enzyme
1.9
D-arabinose 5-phosphate
pH 7.5, 37°C, Cd2+ mutant enzyme N26C
1.9
D-arabinose 5-phosphate
pH 7.5, 37°C, Mn2+ mutant enzyme N26C
2
D-arabinose 5-phosphate
-
pH 7.5, 90°C
2.7
D-arabinose 5-phosphate
at 30°C
3
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R
4
D-arabinose 5-phosphate
-
60°C, pH 7.0, 0.48 mM Cd2+
4.4
D-arabinose 5-phosphate
-
mutant P245A, pH 7.2, 37°C
4.8
D-arabinose 5-phosphate
-
wild-type, pH 7.2, 37°C
4.8
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
4.8
D-arabinose 5-phosphate
-
mutant D243E, pH 7.2, 37°C
4.8
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, R117K
5.31
D-arabinose 5-phosphate
-
pH 6.5, 25°C
5.6
D-arabinose 5-phosphate
-
pH 7.4, 37°C, wild-type enzyme
5.9
D-arabinose 5-phosphate
-
37°C
5.9
D-arabinose 5-phosphate
pH and temperature not specified in the publication, recombinant enzyme
6.1
D-arabinose 5-phosphate
pH 7.5, 37°C, wild-type enzyme
6.1
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114A
6.8
D-arabinose 5-phosphate
-
pH 7.6, 37°C
6.8
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication
8
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
8
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, wild/type enzyme
8.6
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F139A
9
D-arabinose 5-phosphate
pH 7.5, 60°C, wild-type Mn2+-enzyme
0.02
phosphoenolpyruvate
N23C/C246S mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.095
phosphoenolpyruvate
-
0.1
phosphoenolpyruvate
-
pH 7.8, Co2+-reconstituted enzyme
0.1
phosphoenolpyruvate
-
pH 7.8, Cu2+-reconstituted enzyme
0.3
phosphoenolpyruvate
-
pH 7.8, Zn2+-reconstituted enzyme
0.31
phosphoenolpyruvate
N23C/C247E/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.31
phosphoenolpyruvate
recombinant enzyme produced in Escherichia coli, native Zn2+ and Fe2+ not substituted, 100 mM Tris-acetate, pH 7.5, 40°C
0.32
phosphoenolpyruvate
mutant enzyme R106G
0.333
phosphoenolpyruvate
-
0.34
phosphoenolpyruvate
enzyme preparation 1, substitution with 5 microM Cu2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.36
phosphoenolpyruvate
pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated
0.36
phosphoenolpyruvate
enzyme preparation 1, substitution with 5 microM Cu2+, pH 5.0, 40°C
0.38
phosphoenolpyruvate
-
pH 7.5, 60°C
0.38
phosphoenolpyruvate
N23C/C247E mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.38
phosphoenolpyruvate
N23C/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.41
phosphoenolpyruvate
enzyme preparation 1, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.42
phosphoenolpyruvate
pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated
0.46
phosphoenolpyruvate
independent enzyme preparation 2, substitution with 50 microM Cd2+, pH 5.0, 40°C
0.47
phosphoenolpyruvate
enzyme preparation 1, substitution with 50 microM Zn2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.48
phosphoenolpyruvate
wild-type enzyme
0.48
phosphoenolpyruvate
independent preparation 2 enzyme, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C
0.49
phosphoenolpyruvate
-
pH 6.5, 25°C, Zn2+-enzyme
0.72
phosphoenolpyruvate
-
pH 7.4, 25°C, mutant enzyme P145S
0.87
phosphoenolpyruvate
-
pH 7.5, 70°C
0.93
phosphoenolpyruvate
N23C mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.94
phosphoenolpyruvate
N23C/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
1
phosphoenolpyruvate
-
pH 7.4, 37°C
1
phosphoenolpyruvate
-
pH 7.8, Cd2+-reconstituted enzyme
1.08
phosphoenolpyruvate
-
pH 6.5, 25°C, Cd2+-enzyme
1.42
phosphoenolpyruvate
N23C mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
1.47
phosphoenolpyruvate
-
pH 7.5, 80°C
1.9
phosphoenolpyruvate
pH 7.5, 37°C, Cd2+ mutant enzyme N26C
1.9
phosphoenolpyruvate
pH 7.5, 37°C, Mn2+ mutant enzyme N26C
2
phosphoenolpyruvate
-
pH 7.5, 90°C
2.02
phosphoenolpyruvate
-
pH 7.4, 37°C, mutant enzyme P145S
2.02
phosphoenolpyruvate
N23C/C247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
2.08
phosphoenolpyruvate
-
pH 7.4, 25°C, wild-type enzyme
2.71
phosphoenolpyruvate
N23C/C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
3.27
phosphoenolpyruvate
N23C/C247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
3.6
phosphoenolpyruvate
D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
3.9
phosphoenolpyruvate
N23C/C246S/D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
4
phosphoenolpyruvate
-
60°C, pH 7.0, 0.48 mM Cd2+
4.4
phosphoenolpyruvate
D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
4.4
phosphoenolpyruvate
N23C/C246S/D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
4.79
phosphoenolpyruvate
N23C/C246S/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
5.31
phosphoenolpyruvate
-
pH 6.5, 25°C
5.5
phosphoenolpyruvate
C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
5.9
phosphoenolpyruvate
-
37°C
5.9
phosphoenolpyruvate
pH and temperature not specified in the publication, recombinant enzyme
6.1
phosphoenolpyruvate
pH 7.5, 37°C, wild-type enzyme
6.7
phosphoenolpyruvate
-
pH 7.4, 37°C, wild-type enzyme
6.8
phosphoenolpyruvate
-
pH and temperature not specified in the publication
8
phosphoenolpyruvate
wild type, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
8.6
phosphoenolpyruvate
P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
9
phosphoenolpyruvate
pH 7.5, 60°C, wild-type Mn2+-enzyme
100
phosphoenolpyruvate
-
in 10 mM ammonium acetate buffer, pH 7.8
additional information
additional information
N23C/C246S/D247E mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/D247E mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
N23C/C246S/D247E/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/D247E/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
N23C/C246S/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.016 - 0.57
2-deoxy-D-ribose 5-phosphate
0.016 - 1400
D-arabinose 5-phosphate
0.4 - 3200
phosphoenolpyruvate
additional information
additional information
-
0.016
2-deoxy-D-ribose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.13
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.13
2-deoxy-D-ribose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
0.57
2-deoxy-D-ribose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
0.016
D-arabinose 5-phosphate
-
mutant N59DELTA, pH 7.5, temperature not specified in the publication
0.02
D-arabinose 5-phosphate
N23C/C246S mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.029
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R
0.039
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R/R117Q
0.1
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114R/R117A
0.29
D-arabinose 5-phosphate
-
mutant N59A, pH 7.5, temperature not specified in the publication
0.33
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, R117Q
0.9
D-arabinose 5-phosphate
N23C/C247E/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1.6
D-arabinose 5-phosphate
N23C/C247E mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1.8
D-arabinose 5-phosphate
-
mutant D243E, pH 7.2, 37°C
3.5
D-arabinose 5-phosphate
N23C/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
3.7
D-arabinose 5-phosphate
-
mutant N57A, pH 7.5, temperature not specified in the publication
5.9
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, F114R/R117Q/F139G
7
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F139A
7.9
D-arabinose 5-phosphate
N23C/C246S/D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
8.1
D-arabinose 5-phosphate
N23C/C246S/D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
11
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication, mutant F114A
14
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication
16
D-arabinose 5-phosphate
N23C mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
19
D-arabinose 5-phosphate
N23C/C247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
23
D-arabinose 5-phosphate
N23C/C247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
25
D-arabinose 5-phosphate
N23C/C246S/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
26
D-arabinose 5-phosphate
C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
28
D-arabinose 5-phosphate
N23C/C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
49
D-arabinose 5-phosphate
D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
72
D-arabinose 5-phosphate
N23C/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
73
D-arabinose 5-phosphate
D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
118
D-arabinose 5-phosphate
N23C mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
180
D-arabinose 5-phosphate
-
mutant P245A, pH 7.2, 37°C
220
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
230
D-arabinose 5-phosphate
-
wild-type, pH 7.2, 37°C
660
D-arabinose 5-phosphate
-
pH and temperature not specified in the publication
660
D-arabinose 5-phosphate
-
wild-type, pH 7.5, temperature not specified in the publication
717
D-arabinose 5-phosphate
P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1400
D-arabinose 5-phosphate
wild type, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.4
phosphoenolpyruvate
N23C/C246S mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
18
phosphoenolpyruvate
N23C/C247E/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
49
phosphoenolpyruvate
N23C/C247E mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
115
phosphoenolpyruvate
N23C/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
200
phosphoenolpyruvate
N23C/C246S/D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
247
phosphoenolpyruvate
N23C/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
257
phosphoenolpyruvate
N23C/C246S/D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
263
phosphoenolpyruvate
N23C mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
332
phosphoenolpyruvate
N23C mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
370
phosphoenolpyruvate
-
mutant D243E, pH 7.2, 37°C
400
phosphoenolpyruvate
-
wild-type, pH 7.2, 37°C
411
phosphoenolpyruvate
N23C/C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
424
phosphoenolpyruvate
D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
504
phosphoenolpyruvate
N23C/C246S/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
591
phosphoenolpyruvate
C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
748
phosphoenolpyruvate
N23C/C247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
850
phosphoenolpyruvate
-
mutant P245A, pH 7.2, 37°C
898
phosphoenolpyruvate
D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1363
phosphoenolpyruvate
N23C/C247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
1830
phosphoenolpyruvate
P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
3200
phosphoenolpyruvate
wild type, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
additional information
additional information
N23C/C246S/D247E mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/D247E mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
N23C/C246S/D247E/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/D247E/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
N23C/C246S/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
additional information
additional information
-
N23C/C246S/P249A mutant control is barely active, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.06
N23C/C246S/P249A mutant control, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.19
N23C/C246S mutant control, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.3
N23C/C247E mutant control, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.35
N23C/C247E/P249A mutant control, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.6
crude cell lysate, at 25°C and pH 7.5
0.76
N23C/P249A mutant control, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
1.9
N23C mutant control, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
10.1
C246S mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
11.7
P249A mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
12
wild type, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
2
purified enzyme, at 25°C and pH 7.5
2.34
N23C/P249A mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
2.9
N23C mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
3.1
N23C/C247E mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
4.34
N23C/C247E/P249A mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
5
N23C/C246S mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
5.64
N23C/C246S/D247E/P249A mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
6.3
D247E/P249A mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
6.39
D247E mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
8.4
N23C/C246S/D247E mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
9.8
N23C/C246S/P249A mutant, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O
0.01
N23C/C246S/D247E mutant control, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
0.01
N23C/C246S/D247E/P249A mutant control, 200 microM phosphoenolpyruvate, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA
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A56P/N57DELTA
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
C21N
-
complete loss of activity
D243A
-
mutation of the absolutely conserved 243AspGlyPro245 motif, complete loss of activity
D243Q
-
mutation of the absolutely conserved 243AspGlyPro245 motif, active enzyme with altered metal-dependency
K55A
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
N57A
-
mutation in the absolutely conserved KANRS motif. About 2% of wild-type activity
N57DELTA
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
P245A
-
mutation of the absolutely conserved 243AspGlyPro245 motif, active enzyme with altered metal-dependency
C11N
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability
C11N/S235P/Q237A
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability
H185G
mutation decreases the affinity of the enzyme to bind Fe2+, but not Zn2+. Maximal activity, about 8-10% of the wild-type activity is obtained when the native metal is replaced with Cd2+
P10M/C11N
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability
P10M/C11N/S235P/Q237A
mutant is not capable of binding metal and lacks the structural asymmetry among subunits with regard to substrate binding and conformation of the L7 loop, shows decreased thermal stability
R106G
the closure of the L7 loop is impaired. The mutant enzyme shows a smaller KM-value for phosphoenolpyruvate, larger Ki-value and KM-value for D-arabinose 5-phosphate and smaller Ki-values for phosphate and 2-dehydro-3-deoxy-D-octonate 8-phosphate compared ti wild-type enzyme
C11A
-
mutant enzyme retains less than 1% of the wild-type activity and is incapable of metal binding. Activity is not stimulated by Mn2+, Co2+ and Zn2+. Cd2+ stimulates 2fold at a concentration above 1 mM
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
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+
H204A
site-directed mutagenesis, crystal structure analysis
A56P/N57DELTA
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
F114A
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
F114R
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type, structure analysis
F114R/R117A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type, structure analysis
F114R/R117Q
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
F114R/R117Q/F139G
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
F139G
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
K57A
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
N57D
-
mutation in the absolutely conserved KANRS motif. Complete loss of activity
N59DELTA
-
mutation in the absolutely conserved KANRS motif. Less than 0.1% of wild-type activity
R117K
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
R117Q
-
site-directed mutagenesis, conversion to the corresponding residue in enzyme DAH7PS, EC 2.5.1.54, the mutant shows altered kinetics compared to the wild-type, structure analysis
P145S
-
natural mutation in the temperature-sensitive strain AG701i50 leads to an increase in Km-value for both substrates, D-arabinose 5-phosphate and phosphoenolpyruvate, this mutant enzyme also has an altered oligomeric state. Reduced activity, about 35% of the wild-type, between 15 and 30°C. Above 30°C the activity of the mutant enzyme decreases dramatically
N59A
mutant retains less than 1% of the wild type activity
N59A
-
mutation in the absolutely conserved KANRS motif. About 0.2% of wild-type activity
additional information
gene kdsA1 single knockout and kdsA1/kdsA2 double knockout mutant constructions
additional information
gene kdsA1 single knockout and kdsA1/kdsA2 double knockout mutant constructions
additional information
gene kdsA2 single knockout and kdsA1/kdsA2 double knockout mutant constructions
additional information
gene kdsA2 single knockout and kdsA1/kdsA2 double knockout mutant constructions
additional information
replacement of asparagine with metal-binding cysteine is not sufficient to produce a metal-dependent mutant, 3 to 4 mutations establish a fully functional obligate metal-dependent KDO8PS, metal-dependent mutants containing the C246S exchange are activated in the presence of Mn2+ and Cd2+ to specific activities comparable to the wild type, other metal-dependent mutations show lower activation levels, high concentrations can have inhibitory effects, Mg2+, Ca2+, Ni2+, Sr2+, and Ba2+ have little or no effect on activity, Co2+ and Fe2+ have varying effects, Zn2+ is inhibitory for all cloned enzymes
additional information
-
replacement of asparagine with metal-binding cysteine is not sufficient to produce a metal-dependent mutant, 3 to 4 mutations establish a fully functional obligate metal-dependent KDO8PS, metal-dependent mutants containing the C246S exchange are activated in the presence of Mn2+ and Cd2+ to specific activities comparable to the wild type, other metal-dependent mutations show lower activation levels, high concentrations can have inhibitory effects, Mg2+, Ca2+, Ni2+, Sr2+, and Ba2+ have little or no effect on activity, Co2+ and Fe2+ have varying effects, Zn2+ is inhibitory for all cloned enzymes
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Acinetobacter calcoaceticus, Allium cepa, Brassica oleracea, Cucumis sativus, Daucus carota, Ipomoea batatas, Nicotiana sylvestris, no activity in Malus sp., Solanum tuberosum, Spinacia oleracea
-
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Aggregatibacter actinomycetemcomitans, Bordetella bronchiseptica, Aquifex aeolicus, Aquifex aeolicus (O66496), Arabidopsis thaliana, Porphyromonas gingivalis, Bordetella pertussis, Campylobacter jejuni, Caulobacter vibrioides, Chlorobaculum tepidum, Helicobacter pylori, Helicobacter pylori (Q9ZN55), Klebsiella pneumoniae, Pasteurella multocida, Yersinia pestis, Pisum sativum, Shewanella putrefaciens, Salmonella enterica subsp. enterica serovar Typhi, Vibrio cholerae serotype O1, Actinobacillus pleuropneumoniae (O68662), Escherichia coli (P0A715), Escherichia coli, Chlamydia trachomatis (P0CD74), Haemophilus influenzae (P45251), Mannheimia haemolytica (P95514), Chlamydia psittaci (Q46225), Neisseria meningitidis (Q9XAZ3), Neisseria gonorrhoeae (Q9XB02), Chlamydia pneumoniae (Q9Z7I4), Rickettsia prowazekii (Q9ZE84), Pseudomonas aeruginosa (Q9ZFK4)
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Escherichia coli (P0A715), Escherichia coli
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Helicobacter pylori 3-deoxy-D-manno-octulosonate-8-phosphate (KDO-8-P) synthase is a zinc-metalloenzyme
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Escherichia coli, Helicobacter pylori
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A single point mutation in 3-deoxy-D-manno-octulosonate-8-phosphate synthase is responsible for temperature sensitivity in a mutant strain of Salmonella typhimurium
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Functional and biochemical characterization of a recombinant 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase from the hyperthermophilic bacterium Aquifex aeolicus
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Escherichia coli
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Probing the role of tightly bound phosphoenolpyruvate in Escherichia coli 3-deoxy-d-manno-octulosonate 8-phosphate synthase catalysis using quantitative time-resolved electrospray ionization mass spectrometry in the millisecond time range
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Arabinose 5-phosphate analogues as mechanistic probes for Neisseria meningitidis 3-deoxy-D-manno-octulosonate 8-phosphate synthase
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Neisseria meningitidis (Q9JZ55), Neisseria meningitidis
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The synthesis of the rhamnogalacturonan II component 3-deoxy-D-manno-2-octulosonic acid (Kdo) is required for pollen tube growth and elongation
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59
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Arabidopsis thaliana (Q9AV97)
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Electronic structure of the metal center in the Cd(2+), Zn(2+), and Cu(2+) substituted forms of KDO8P synthase: implications for catalysis
Biochemistry
48
3610-3630
2009
Aquifex aeolicus (O66496), Aquifex aeolicus
brenda
Li, Z.; Sau, A.
Probing the subunit-subunit interaction of the tetramer of E. coli KDO8P synthase by electrospray ionization mass spectrometry
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27
111-116
2009
Escherichia coli (P0A715)
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