Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
2-deoxy-D-glucose 6-phosphate + NAD+
?
-
low activity
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
6-phospho-D-glucono-1,5-lactone + NADH + H+
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
D-glucose 6-phosphate + NADP+
-
-
-
r
D-galactose 6-phosphate + NAD+
?
-
low activity
-
-
?
D-glucose 6-phosphate + NAD(P)+
6-phospho-D-glucono-1,5-lactone + NAD(P)H + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
D-glucose 6-phosphate + NADP+ 2',3'-dialdehyde
6-phospho-D-glucono-1,5-lactone + NADPH 2',3'-dialdehyde + H+
-
-
-
-
?
D-glucose 6-phosphate + thionicotinamide-NAD+
6-phospho-D-glucono-1,5-lactone + thionicotinamide-NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + thionicotinamide-NADP+
6-phospho-D-glucono-1,5-lactone + thionicotinamide-NADPH + H+
-
-
-
-
?
D-glucose 6-sulfate + NAD+
?
-
low activity
-
-
?
additional information
?
-
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
the enzyme generates NADPH, an essential cofactor for several biosynthetic pathways and antioxidant enzymes
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
the enzyme generates NADPH, an essential cofactor for several biosynthetic pathways and antioxidant enzymes
-
-
?
6-phospho-D-glucono-1,5-lactone + NADH + H+
D-glucose 6-phosphate + NAD+
-
-
-
r
6-phospho-D-glucono-1,5-lactone + NADH + H+
D-glucose 6-phosphate + NAD+
-
-
-
r
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
721400, 721401, 721402, 721406, 721411, 721511, 721570, 721573, 721580, 721584, 722578, 722590, 740878 -
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
iso ordered bi bi reaction
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
NAD+, NADP+, and pyridoxylation produce different conformational changes in the enzyme
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
steady-state random mechanism
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
the mechanism with NAD+ is more complex compared to the reaction with D-glucose 6-phosphate and NADP+
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
r
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
r
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
721400, 721401, 721402, 721406, 721411, 721511, 721570, 721573, 721580, 721584, 722476, 722578, 722590, 740878 -
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
NAD+, NADP+, and pyridoxylation produce different conformational changes in the enzyme
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
ordered bi bi reaction
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
ordered, sequential mechanism for this reaction in which NADP+ is bound first to the enzyme and NADPH released last
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
ordered, sequential mechanism. NADP+ binds first
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
r
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
r
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
additional information
?
-
the reaction catalyzed by PputG6PDH-1 yields around 1/3 mol of NADPH and 2/3 mol of NADH per mol of oxidized glucose 6-phosphate, calculation of in vivo relative production of NADH and NADPH during the oxidation of glucose-6-phosphate. The reaction catalyzes by the 6-phosphogluconate dehydrogenase is active during growth on glucose, and it produces NADPH and NADH. In comparison, for the enzyme of Escherichia coli EcG6PDH, the relative production of NADH over NADPH is 1000times lower than for PputG6PDH-1
-
-
?
additional information
?
-
the reaction catalyzed by PputG6PDH-1 yields around 1/3 mol of NADPH and 2/3 mol of NADH per mol of oxidized glucose 6-phosphate. PputG6PDH-1 is not considered a NADP+-specific enzyme
-
-
?
additional information
?
-
the reaction catalyzed by PputG6PDH-1 yields around 1/3 mol of NADPH and 2/3 mol of NADH per mol of oxidized glucose 6-phosphate, calculation of in vivo relative production of NADH and NADPH during the oxidation of glucose-6-phosphate. The reaction catalyzes by the 6-phosphogluconate dehydrogenase is active during growth on glucose, and it produces NADPH and NADH. In comparison, for the enzyme of Escherichia coli EcG6PDH, the relative production of NADH over NADPH is 1000times lower than for PputG6PDH-1
-
-
?
additional information
?
-
the reaction catalyzed by PputG6PDH-1 yields around 1/3 mol of NADPH and 2/3 mol of NADH per mol of oxidized glucose 6-phosphate. PputG6PDH-1 is not considered a NADP+-specific enzyme
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
additional information
?
-
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NAD+
D-ribulose 5-phosphate + CO2 + NADH + H+
-
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
the enzyme generates NADPH, an essential cofactor for several biosynthetic pathways and antioxidant enzymes
-
-
?
6-phospho-D-gluconate + NADP+
D-ribulose 5-phosphate + CO2 + NADPH + H+
the enzyme generates NADPH, an essential cofactor for several biosynthetic pathways and antioxidant enzymes
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
r
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
r
D-glucose 6-phosphate + NAD+
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
r
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
r
D-glucose 6-phosphate + NADP+
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
-
?
additional information
?
-
the reaction catalyzed by PputG6PDH-1 yields around 1/3 mol of NADPH and 2/3 mol of NADH per mol of oxidized glucose 6-phosphate, calculation of in vivo relative production of NADH and NADPH during the oxidation of glucose-6-phosphate. The reaction catalyzes by the 6-phosphogluconate dehydrogenase is active during growth on glucose, and it produces NADPH and NADH. In comparison, for the enzyme of Escherichia coli EcG6PDH, the relative production of NADH over NADPH is 1000times lower than for PputG6PDH-1
-
-
?
additional information
?
-
the reaction catalyzed by PputG6PDH-1 yields around 1/3 mol of NADPH and 2/3 mol of NADH per mol of oxidized glucose 6-phosphate, calculation of in vivo relative production of NADH and NADPH during the oxidation of glucose-6-phosphate. The reaction catalyzes by the 6-phosphogluconate dehydrogenase is active during growth on glucose, and it produces NADPH and NADH. In comparison, for the enzyme of Escherichia coli EcG6PDH, the relative production of NADH over NADPH is 1000times lower than for PputG6PDH-1
-
-
?
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.
2',5'-ADP
-
NADP+-competitive and NAD+-noncompetitive inhibition
4-hydroxy-2-nonenal
-
pseudo first-order loss of enzyme activity. The pH dependence of the inactivation rate exhibits an inflection around pH 10, and the enzyme is protected from inactivation by glucose 6-phosphate. Loss of enzyme activity corresponds with the formation of one carbonyl function per enzyme subunit and the appearance of a lysine-4-hydroxy-2-nonenal adduct
cis-9-octadecenoyl-CoA
-
2.0 mM, 9% inhibition of NADP+-dependent reaction, 90% inhibition of NAD+-dependent reaction
citrate
-
incubation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides with Fe2+ and citrate results in rapid O2-dependent inactivation of the enzyme. The Fe(2+)-citrate complex binds to the glucose 6-phosphate binding site and then undergoes reaction with H2O2 formed in solution leading to the oxidative modification of amino acids essential for enzyme activity
CoA
-
3.4 mM, 12% inhibition of NADP+-dependent reaction, 82% inhibition of NAD+-dependent reaction
Cu2+
-
1 mM, 57% loss of activity. 5 mM, 64.8% loss of activity
D-glucose 1-phosphate
-
a substrate-competitive inhibitor, that lowers the dissociation constant and maximum fluorescence quenching for NAD+ but not for NADP+
D-glucose 6-phosphate
-
high concentrations inhibit the NADP+-linked reaction in the dual wavelength assay (a method employing a mixture of one coenzyme and the thionicotinamide analog of the other coenzyme). Such inhibition is not observed in conventional assays using either NADP+ or thionicotinamide-NADP+
Fe3+
-
1 mM, 47.3% loss of activity. 5 mM, 95.2% loss of activity
H2O2
-
the enzyme is rapidly inactivated by micromolar concentrations of Fe2+ and H2O2. Inactivation correlates with the formation of one carbonyl functionality/enzyme subunit, indicating that inactivation is the result of site-specific oxidative modification. Fe2+ binds to the glucose 6-phosphate binding site and interaction of the enzyme-bound Fe2+ with H2O2 leads to the oxidative modification of amino acids essential for enzyme activity. Partially inactivated enzyme remains predominantly in the dimeric form, and no change in the apparent affinity of the remaining active subunits for substrate is observed. Partial inactivation leads to a decrease in the thermal stability of the remaining activity. This decrease in thermal stability could be largely overcome by the addition of glucose 6-phosphate. Thus, although exposure to H2O2 and Fe2+ results in the irreversible inactivation of the enzyme, the resulting modification is selective, leads to the formation of heterodimers of both active and inactive subunits, and does not appear to cause large scale structural changes
malonyl-CoA
-
2.4 mM, no inhibition of NADP+-dependent reaction, 14% inhibition of NAD+-dependent reaction
N'-methylnicotinamide
-
-
NADP+ 2',3'-dialdehyde
-
irreversible inactivation in absence of substrate. The inactivation is first order with respect to NADP+ concentration and follows saturation kinetics, indicating that the enzyme initially forms a reversible complex with the inhibitor followed by covalent modification. NADP+ and NAD+ protect the enzyme from inactivation. One molecule of NADP+ 2',3'-dialdehyde binds per subunit of glucose-6-phosphate dehydrogenase when the enzyme is completely inactivated
Ni2+
-
1 mM, 71.4% loss of activity. Complete loss of activity
palmitoyl-CoA
-
inhibition is greatly diminished at high glucose 6-phosphate concentration
pyridoxal 5'-diphospho-5'-adenosine
-
inhibits competitively with respect to glucose 6-phosphate and noncompetitively with respect to NAD+ or NADP+. 0.85 mol of pyridoxal 5'-diphospho-5'-adenosine is required for complete inactivation. Lys21 and Lys343 are the sites of pyridoxal 5'-diphospho-5'-adenosine interaction. Both glucose 6-phosphate and NAD+ protect both lysyl residues against this covalent modification
vanadate
-
inhibition by vanadate dimer and tetramer. The inhibition by vanadate is competitive with respect to NAD+ or NADP+ and noncompetitive (a mixed type) with respect to glucose 6-phosphate when NAD+ or NADP+ are cofactors. The vanadate dimer is the major inhibiting species with respect to NADP+. The vanadate tetramer is the major inhibiting species with respect to glucose 6-phosphate and with respect to NAD+. No inhibition by monomeric vanadate
Zn2+
-
1 mM, 57% loss of activity. 5 mM, 93% loss of activity
additional information
-
no inhibition by iodoacetate, iodoacetamide, and p-hydroxymercuribenzoate
-
acetyl-CoA
-
inhibition is greatly diminished at high glucose 6-phosphate concentration
acetyl-CoA
-
2.6 mM, no inhibition of NADP+-dependent reaction, 70% inhibition of NAD+-dependent reaction
ATP
-
-
ATP
-
inhibition is greatly diminished at high glucose 6-phosphate concentration
ATP
-
the kinetics of ATP inhibition of the NAD+- and NADP+-linked reactions examined at pH 6.2 and pH 7.8. The results are interpreted in terms of ATP addition to binary enzyme-coenzyme and enzyme-glucose 6-phosphate complexes
ATP
-
3.9 mM, 50% inhibition of NADP+-dependent reaction, 90% inhibition of NAD+-dependent reaction
ATP
-
inhibits competitively with respect to thionicotinamide-NAD+
Fe2+
-
incubation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides with Fe2+ and citrate results in rapid O2-dependent inactivation of the enzyme. The Fe(2+)-citrate complex binds to the glucose 6-phosphate binding site and then undergoes reaction with H2O2 formed in solution leading to the oxidative modification of amino acids essential for enzyme activity
Fe2+
-
the enzyme is rapidly inactivated by micromolar concentrations of Fe2+ and H2O2. Inactivation correlates with the formation of one carbonyl functionality/enzyme subunit, indicating that inactivation is the result of site-specific oxidative modification. Fe2+ binds to the glucose 6-phosphate binding site and interaction of the enzyme-bound Fe2+ with H2O2 leads to the oxidative modification of amino acids essential for enzyme activity. Partially inactivated enzyme remains predominantly in the dimeric form, and no change in the apparent affinity of the remaining active subunits for substrate is observed. Partial inactivation leads to a decrease in the thermal stability of the remaining activity. This decrease in thermal stability could be largely overcome by the addition of glucose 6-phosphate. Thus, although exposure to H2O2 and Fe2+ results in the irreversible inactivation of the enzyme, the resulting modification is selective, leads to the formation of heterodimers of both active and inactive subunits, and does not appear to cause large scale structural changes
NAD+
-
-
NADH
-
product inhibition. With NAD+ as the varied substrate and glucose 6-phosphate, nonsaturating, linear noncompetitive inhibition is observed. When an experiment is performed using saturating glucose 6-phosphate, the inhibition again appears to be noncompetitive. When glucose 6-phosphate is the varied substrate inhibition by NADH appears to be noncompetitive whether NAD+ is nonsaturating or saturating
NADH
-
inhibits noncompetitively with respect to thionicotinamide-NAD+
NADH
competitive inhibition
NADP+
-
increasing NADPH/NADP+ concentration ratios inhibit the NADP-linked, but stimulate the NAD-linked reaction
NADP+
mixed-type inhibition
NADPH
-
increasing NADPH/NADP+ concentration ratios inhibit the NADP-linked, but stimulate the NAD-linked reaction
NADPH
-
NADPH is tested as an alternate product inhibitor for the NAD+-linked reaction. With glucose 6-phosphate saturating and NAD+ varied the inhibition is linear noncompetitive
NADPH
-
inhibits competitively with respect to thionicotinamide-NADP+
NADPH
inhibits competitively when NADP+ is the varying substrate and noncompetitively when D-glucose 6-phosphate is the varying substrate
pyridoxal 5'-phosphate
-
inhibition in phosphate buffers at pH 7.7 and pH 6.3. 0.1 mM Pyridoxal 5-phosphate produces 50% inhibition at pH 7.7. At the lower pH more pyridoxal 5-phosphate is required to give the same degree of inhibition. The enzyme must be incubated with pyridoxal 5-phosphate prior to assaying in order to achieve maximum inhibition. Pyridoxamine 5-phosphate and pyridoxal are only slightly inhibitory. When glucose 6-phosphate is varied at a constant, nearly saturating concentration of NAD+ pyridoxal 5-phosphate behaves like a competitive inhibitor. When NAD+ is varied and glucose 6-phosphate maintained at nearly saturating concentration, inhibition by pyridoxal 5-phosphate is noncompetitive
pyridoxal 5'-phosphate
-
modifies Lys21 and probably Lys343
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.
12
2-deoxy-D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+
10
D-galactose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+
0.007 - 106
D-glucose 6-phosphate
50
D-glucose 6-sulfate
-
25°C, pH 7.8, cosubstrate: NAD+
200
NADP+ 2',3'-dialdehyde
-
25°C, pH 7.8
0.011
thionicotinamide-NAD+
0.001
thionicotinamide-NADP+
-
pH 7.8, 25°C
additional information
additional information
-
0.007
D-glucose 6-phosphate
-
pH 7.8, 25°C, cosubstrate: thionicotinamide-NAD+
0.009
D-glucose 6-phosphate
-
pH 7.8, 25°C, cosubstrate: thionicotinamide-NADP+
0.05
D-glucose 6-phosphate
-
25°C, pH 6.2, NADP+-linked reaction
0.053
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+
0.053
D-glucose 6-phosphate
-
25°C, pH 7.8, NAD+-linked reaction
0.053
D-glucose 6-phosphate
-
pH 7.8, 25°C, cosubstrate: NAD+
0.063
D-glucose 6-phosphate
-
25°C, pH 6.7, NADP+-linked reaction
0.063
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Y415F
0.066
D-glucose 6-phosphate
-
25°C, pH 6.8, NAD+-linked reaction
0.068
D-glucose 6-phosphate
-
25°C, pH 6.3, NAD+-linked reaction
0.069
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, wild-type enzyme
0.0692
D-glucose 6-phosphate
-
wild type enzyme, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.073
D-glucose 6-phosphate
-
25°C, pH 7.1, cosubstrate: NADP+
0.074
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Y415F
0.075
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme T14S
0.075
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Q47A
0.078
D-glucose 6-phosphate
-
25°C, pH 7.8, NAD+-dependent reaction
0.081
D-glucose 6-phosphate
-
25°C, pH 7.2, cosubstrate: NADP+
0.081
D-glucose 6-phosphate
-
25°C, pH 7.2, NADP+-linked reaction
0.081
D-glucose 6-phosphate
-
pH 7.8, 25°C, cosubstrate: NADP+
0.089
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46Q
0.0891
D-glucose 6-phosphate
-
mutant enzyme R46Q, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.09
D-glucose 6-phosphate
-
25°C, pH 7.8, NADP+-dependent reaction
0.096
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Q47A
0.097
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme K21R
0.114
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, wild-type enzyme
0.114
D-glucose 6-phosphate
-
wild type enzyme, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.117
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme D177N
0.118
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme T14S
0.13
D-glucose 6-phosphate
-
20°C, NADP+-linked reaction, pH not specified in the publication
0.132
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme R46E
0.135
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme D374Q
0.145
D-glucose 6-phosphate
-
30°C, NADP+-linked reaction, pH not specified in the publication
0.165
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Y179F
0.169
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme T14A
0.175
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46A
0.175
D-glucose 6-phosphate
-
mutant enzyme R46A, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.181
D-glucose 6-phosphate
-
free enzyme, with NADP+ as cosubstrate, at pH 7.5 and 37°C
0.193
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme D374Q
0.21
D-glucose 6-phosphate
-
25°C, pH 7.1, cosubstrate: NAD+
0.228
D-glucose 6-phosphate
-
tetraethyl orthosilicate-gel-immobilized enzyme, with NADP+ as cosubstrate, at pH 7.5 and 37°C
0.233
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Q47E
0.239
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme K21R
0.239
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Q47E
0.29
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme D177N
0.334
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46Q
0.334
D-glucose 6-phosphate
-
mutant enzyme R46Q, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.378
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme T14A
0.441
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Y179F
0.467
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant
0.467
D-glucose 6-phosphate
-
mutant enzyme R46A, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.675
D-glucose 6-phosphate
-
20°C, NAD+-linked reaction, pH not specified in the publication
0.8
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme H240N
0.825
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme P149G
0.946
D-glucose 6-phosphate
-
with NADP+ as cosubstrate, at pH 8.0 and 30°C
0.946
D-glucose 6-phosphate
pH 8.0, 30°C, recombinant enzyme, with NADP+
1.04
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme R46E
1.08
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme P149V
1.137
D-glucose 6-phosphate
-
with NAD+ as cosubstrate, at pH 8.0 and 30°C
1.137
D-glucose 6-phosphate
pH 8.0, 30°C, recombinant enzyme, with NAD+
1.28
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme H240N
1.3
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K343R
1.73
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme P149V
2.5
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme K21Q
2.6
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme P149G
3.08
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K343R
3.7
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K182R
4.3
D-glucose 6-phosphate
-
30°C, NAD+-linked reaction, pH not specified in the publication
6.07
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme K21Q
6.8
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K182Q
13.1
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K182Q
13.6
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme H1787N
16.1
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K182R
25.3
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K343Q
42.9
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme H1787N
106
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K343Q
0.053
NAD+
-
at pH 7.5 and 32°C
0.082
NAD+
-
25°C, pH 7.8, mutant enzyme K182Q
0.102
NAD+
-
25°C, pH 7.8
0.106
NAD+
-
pH 7.8, 25°C
0.106
NAD+
-
25°C, pH 7.8
0.106
NAD+
-
25°C, pH 7.8, cosubstrate: D-glucose 6-phosphate
0.116
NAD+
-
25°C, pH 7.8, mutant enzyme Y415F
0.127
NAD+
pH 8.0, 30°C, recombinant enzyme
0.127
NAD+
-
at pH 8.0 and 30°C
0.16
NAD+
25°C, pH 7.6, wild-type enzyme
0.162
NAD+
-
wild type enzyme, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.184
NAD+
-
25°C, pH 7.8, mutant enzyme Y179F
0.199
NAD+
-
25°C, pH 7.8, mutant enzyme T14S
0.233
NAD+
-
mutant enzyme R46Q, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.234
NAD+
-
25°C, pH 7.8, mutant enzyme Q47A
0.24
NAD+
25°C, pH 7.6, mutant enzyme K21R
0.31
NAD+
-
25°C, pH 7.8, mutant enzyme Q47E
0.338
NAD+
-
25°C, pH 7.8, mutant enzyme K343R
0.359
NAD+
-
25°C, pH 6.8
0.379
NAD+
-
25°C, pH 7.8, mutant enzyme K182R
0.432
NAD+
-
25°C, pH 6.3
0.503
NAD+
-
25°C, pH 7.8, mutant enzyme K343Q
0.52
NAD+
25°C, pH 7.6, mutant enzyme K21Q
0.571
NAD+
-
25°C, pH 7.8, mutant enzyme D374Q
0.81
NAD+
-
25°C, pH 7.6, mutant enzyme H240N
0.95
NAD+
-
25°C, pH 7.6, mutant enzyme H1787N
0.986
NAD+
-
25°C, pH 7.8, mutant enzyme R46E
1.05
NAD+
-
mutant enzyme R46A, in 33 mM Tris-HCl, pH 7.6, at 25°C
1.14
NAD+
-
25°C, pH 7.6, mutant enzyme D177N
1.76
NAD+
-
25°C, pH 7.8, mutant enzyme P149G
2.23
NAD+
-
25°C, pH 7.8, mutant enzyme P149V
2.3
NAD+
-
25°C, pH 7.8, mutant enzyme T14A
0.0042
NADP+
-
25°C, pH 6.2
0.0043
NADP+
-
25°C, pH 6.7
0.0047
NADP+
-
25°C, pH 7.8
0.0057
NADP+
-
25°C, pH 7.2
0.006
NADP+
-
pH 7.8, 25°C
0.006
NADP+
-
25°C, pH 7.2, cosubstrate: D-glucose 6-phosphate
0.0065
NADP+
-
25°C, pH 7.8, mutant enzyme K182Q
0.007
NADP+
25°C, pH 7.6, mutant enzyme K21Q
0.0075
NADP+
-
25°C, pH 7.8, mutant enzyme Q47A
0.00799
NADP+
-
wild type enzyme, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.008
NADP+
25°C, pH 7.6, wild-type enzyme
0.008
NADP+
25°C, pH 7.6, mutant enzyme K21R
0.008
NADP+
-
25°C, pH 7.8, mutant enzyme K343R
0.0082
NADP+
-
25°C, pH 7.6, mutant enzyme D177N
0.0088
NADP+
-
25°C, pH 7.6, mutant enzyme H240N
0.012
NADP+
-
at pH 7.5 and 32°C
0.013
NADP+
-
25°C, pH 7.8, mutant enzyme D374Q
0.014
NADP+
pH 8.0, 30°C, recombinant enzyme
0.014
NADP+
-
at pH 8.0 and 30°C
0.014
NADP+
-
25°C, pH 7.8, mutant enzyme T14S
0.014
NADP+
-
25°C, pH 7.8, mutant enzyme Y179F
0.015
NADP+
-
25°C, pH 7.8, mutant enzyme K182R
0.0152
NADP+
-
25°C, pH 7.6, mutant enzyme H1787N
0.018
NADP+
-
25°C, pH 7.8, mutant enzyme P149V
0.022
NADP+
-
25°C, pH 7.1
0.024
NADP+
-
25°C, pH 7.8, mutant enzyme P149G
0.046
NADP+
-
25°C, pH 7.8, mutant enzyme K343Q
0.063
NADP+
-
25°C, pH 7.8, mutant enzyme Y415F
0.084
NADP+
-
25°C, pH 7.8, mutant enzyme Q47E
0.086
NADP+
-
25°C, pH 7.8, mutant enzyme T14A
0.233
NADP+
-
25°C, pH 7.6, mutant enzyme R46Q
0.854
NADP+
-
25°C, pH 7.6, mutant enzyme R46Q
0.854
NADP+
-
mutant enzyme R46Q, in 33 mM Tris-HCl, pH 7.6, at 25°C
1.05
NADP+
-
25°C, pH 7.6, mutant enzyme R46A
5.57
NADP+
-
mutant enzyme R46A, in 33 mM Tris-HCl, pH 7.6, at 25°C
21
NADP+
-
25°C, pH 7.8, mutant enzyme R46E
0.011
thionicotinamide-NAD+
-
pH 7.8, 25°C
0.011
thionicotinamide-NAD+
-
25°C, pH 7.2, cosubstrate: D-glucose 6-phosphate
additional information
additional information
-
the Km-value of NAD+ is insensitive to ionic strength over the range tested but that the Km for glucose 6-phosphate is affected. This effect is greatest at pH 9.0
-
additional information
additional information
kinetics and modelling, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.007 - 1800
D-glucose 6-phosphate
254
NADH
pH 8.0, 30°C, recombinant enzyme
105
NADPH
pH 8.0, 30°C, recombinant enzyme
0.007
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme H240N
0.02
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme H240N
0.6
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme P149V
1.1
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme D177N
2.7
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme P149V
4.85
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme D177N
8.5
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme P149G
13.8
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme H1787N
14.2
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme H1787N
17.5
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme P149G
19.9
D-glucose 6-phosphate
-
20°C, NAD+-linked reaction, pH not specified in the publication
46.4
D-glucose 6-phosphate
-
30°C, NAD+-linked reaction, pH not specified in the publication
75.2
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme D374Q
100
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme K21Q
116.9
D-glucose 6-phosphate
-
20°C, NADP+-linked reaction, pH not specified in the publication
134.7
D-glucose 6-phosphate
-
30°C, NADP+-linked reaction, pH not specified in the publication
183
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Y415F
208
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme D374Q
235
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Q47A
255
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K182Q
263
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Y179F
308
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K182Q
317
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Y415F
365
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme K21R
378
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme T14S
403
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K343R
475
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Y179F
522
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, wild-type enzyme
522
D-glucose 6-phosphate
-
wild type enzyme, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
552
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Q47E
577
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Q47A
582
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme K21R
583
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme T14S
585
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K182R
632
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme T14A
633
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme R46E
658
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme R46E
712
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K343Q
750
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K343R
808
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Q47E
808
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme T14A
825
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46Q
825
D-glucose 6-phosphate
-
mutant enzyme R46Q, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
850
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K343Q
887
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46Q
887
D-glucose 6-phosphate
-
mutant enzyme R46Q, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
1068
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K182R
1125
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, wild-type enzyme
1125
D-glucose 6-phosphate
-
wild type enzyme, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
1423
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme K21Q
1535
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46A
1535
D-glucose 6-phosphate
-
mutant enzyme R46A, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
1800
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46A
1800
D-glucose 6-phosphate
-
mutant enzyme R46A, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.02
NAD+
-
25°C, pH 7.6, mutant enzyme H240N
2.7
NAD+
-
25°C, pH 7.8, mutant enzyme P149V
4.85
NAD+
-
25°C, pH 7.6, mutant enzyme D177N
14.2
NAD+
-
25°C, pH 7.6, mutant enzyme H1787N
17.5
NAD+
-
25°C, pH 7.8, mutant enzyme P149G
208
NAD+
-
25°C, pH 7.8, mutant enzyme D374Q
255
NAD+
-
25°C, pH 7.8, mutant enzyme K182Q
277
NAD+
pH 8.0, 30°C, recombinant enzyme
277
NAD+
-
at pH 8.0 and 30°C
317
NAD+
-
25°C, pH 7.8, mutant enzyme Y415F
365
NAD+
25°C, pH 7.6, mutant enzyme K21R
475
NAD+
-
25°C, pH 7.8, mutant enzyme Y179F
577
NAD+
-
25°C, pH 7.8, mutant enzyme Q47A
583
NAD+
-
25°C, pH 7.8, mutant enzyme T14S
658
NAD+
-
25°C, pH 7.8, mutant enzyme R46E
750
NAD+
-
25°C, pH 7.8, mutant enzyme K343R
808
NAD+
-
25°C, pH 7.8, mutant enzyme Q47E
808
NAD+
-
25°C, pH 7.8, mutant enzyme T14A
850
NAD+
-
25°C, pH 7.8, mutant enzyme K343Q
1068
NAD+
-
25°C, pH 7.8, mutant enzyme K182R
1125
NAD+
25°C, pH 7.6, wild-type enzyme
1423
NAD+
25°C, pH 7.6, mutant enzyme K21Q
0.007
NADP+
-
25°C, pH 7.6, mutant enzyme H240N
0.6
NADP+
-
25°C, pH 7.8, mutant enzyme P149V
1.1
NADP+
-
25°C, pH 7.6, mutant enzyme D177N
8.5
NADP+
-
25°C, pH 7.8, mutant enzyme P149G
13.8
NADP+
-
25°C, pH 7.6, mutant enzyme H1787N
75.2
NADP+
-
25°C, pH 7.8, mutant enzyme D374Q
100
NADP+
25°C, pH 7.6, mutant enzyme K21Q
102
NADP+
pH 8.0, 30°C, recombinant enzyme
102
NADP+
-
at pH 8.0 and 30°C
183
NADP+
-
25°C, pH 7.8, mutant enzyme Y415F
235
NADP+
-
25°C, pH 7.8, mutant enzyme Q47A
263
NADP+
-
25°C, pH 7.8, mutant enzyme Y179F
308
NADP+
-
25°C, pH 7.8, mutant enzyme K182Q
378
NADP+
-
25°C, pH 7.8, mutant enzyme T14S
403
NADP+
-
25°C, pH 7.8, mutant enzyme K343R
522
NADP+
25°C, pH 7.6, wild-type enzyme
552
NADP+
-
25°C, pH 7.8, mutant enzyme Q47E
582
NADP+
25°C, pH 7.6, mutant enzyme K21R
585
NADP+
-
25°C, pH 7.8, mutant enzyme K182R
632
NADP+
-
25°C, pH 7.8, mutant enzyme T14A
633
NADP+
-
25°C, pH 7.8, mutant enzyme R46E
712
NADP+
-
25°C, pH 7.8, mutant enzyme K343Q
825
NADP+
-
25°C, pH 7.6, mutant enzyme R46Q
887
NADP+
-
25°C, pH 7.6, mutant enzyme R46Q
1535
NADP+
-
25°C, pH 7.6, mutant enzyme R46A
1800
NADP+
-
25°C, pH 7.6, mutant enzyme R46A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.005 - 16250
D-glucose 6-phosphate
0.005
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme H240N
0.025
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme H240N
0.32
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme H1787N
0.5
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme P149V
1.04
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme H1787N
1.7
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme P149V
3.34
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme P149G
6.7
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K343Q
8.9
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Y415F
9.4
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme D177N
10.8
D-glucose 6-phosphate
-
30°C, NAD+-linked reaction, pH not specified in the publication
16.5
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme K21Q
16.7
D-glucose 6-phosphate
-
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme D177N
21.7
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme P149G
23.4
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K182Q
29.5
D-glucose 6-phosphate
-
20°C, NAD+-linked reaction, pH not specified in the publication
33.4
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K343Q
36.7
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K182R
132
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme K343R
284
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K182R
384
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme D374Q
569
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme K21Q
601
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K343R
601
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Y179F
618
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme R46E
899.2
D-glucose 6-phosphate
-
20°C, NADP+-linked reaction, pH not specified in the publication
929
D-glucose 6-phosphate
-
30°C, NADP+-linked reaction, pH not specified in the publication
1553
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme D374Q
1670
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme T14A
2304
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Q47E
2435
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, mutant enzyme K21R
2650
D-glucose 6-phosphate
-
mutant enzyme R46Q, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
2656
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46Q
2889
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Y179F
2956
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NADP+, wild-type enzyme
3140
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme Q47A
3206
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NADP+, mutant enzyme T14S
3474
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Q47E
3762
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, mutant enzyme K21R
3814
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme K182Q
3850
D-glucose 6-phosphate
-
mutant enzyme R46A, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
3854
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46A
4583
D-glucose 6-phosphate
-
wild type enzyme, with NADP+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
4760
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme T14A
4993
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme R46E
5043
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Y415F
6012
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme Q47A
7799
D-glucose 6-phosphate
-
25°C, pH 7.8, cosubstrate: NAD+, mutant enzyme T14S
8767
D-glucose 6-phosphate
-
mutant enzyme R46A, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
8771
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46A
9267
D-glucose 6-phosphate
-
mutant enzyme R46Q, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
9270
D-glucose 6-phosphate
-
25°C, pH 7.6, mutant enzyme R46Q
10540
D-glucose 6-phosphate
25°C, pH 7.6, cosubstrate: NAD+, wild-type enzyme
16250
D-glucose 6-phosphate
-
wild type enzyme, with NAD+ as cosubstrate, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.025
NAD+
-
25°C, pH 7.6, mutant enzyme H240N
1.2
NAD+
-
25°C, pH 7.8, mutant enzyme P149V
4.25
NAD+
-
25°C, pH 7.6, mutant enzyme D177N
10.2
NAD+
-
25°C, pH 7.8, mutant enzyme P149G
14.95
NAD+
-
25°C, pH 7.6, mutant enzyme H1787N
351
NAD+
-
25°C, pH 7.8, mutant enzyme T14A
367
NAD+
-
25°C, pH 7.8, mutant enzyme D374Q
668
NAD+
-
25°C, pH 7.8, mutant enzyme R46E
1462
NAD+
-
mutant enzyme R46A, in 33 mM Tris-HCl, pH 7.6, at 25°C
1687
NAD+
-
25°C, pH 7.8, mutant enzyme K343Q
2181
NAD+
pH 8.0, 30°C, recombinant enzyme
2221
NAD+
-
25°C, pH 7.8, mutant enzyme K343R
2472
NAD+
-
25°C, pH 7.8, mutant enzyme Q47A
2589
NAD+
-
25°C, pH 7.8, mutant enzyme Y179F
2605
NAD+
-
25°C, pH 7.8, mutant enzyme Q47E
2739
NAD+
-
25°C, pH 7.8, mutant enzyme Y415F
2822
NAD+
-
25°C, pH 7.8, mutant enzyme K182R
2939
NAD+
-
25°C, pH 7.8, mutant enzyme T14S
3123
NAD+
-
25°C, pH 7.8, mutant enzyme K182Q
3533
NAD+
-
mutant enzyme R46Q, in 33 mM Tris-HCl, pH 7.6, at 25°C
6950
NAD+
-
wild type enzyme, in 33 mM Tris-HCl, pH 7.6, at 25°C
7031
NAD+
25°C, pH 7.6, wild-type enzyme
0.8
NADP+
-
25°C, pH 7.6, mutant enzyme H240N
5.57
NADP+
-
mutant enzyme R46A, in 33 mM Tris-HCl, pH 7.6, at 25°C
30
NADP+
-
25°C, pH 7.8, mutant enzyme R46E
33.4
NADP+
-
25°C, pH 7.8, mutant enzyme P149V
134.1
NADP+
-
25°C, pH 7.6, mutant enzyme D177N
323
NADP+
-
25°C, pH 7.6, mutant enzyme R46A
323
NADP+
-
mutant enzyme R46Q, in 33 mM Tris-HCl, pH 7.6, at 25°C
351
NADP+
-
25°C, pH 7.8, mutant enzyme P149G
904
NADP+
-
25°C, pH 7.6, mutant enzyme H1787N
1039
NADP+
-
25°C, pH 7.6, mutant enzyme R46Q
1462
NADP+
-
25°C, pH 7.6, mutant enzyme R46A
3540
NADP+
-
25°C, pH 7.6, mutant enzyme R46Q
5778
NADP+
-
25°C, pH 7.8, mutant enzyme D374Q
6579
NADP+
-
25°C, pH 7.8, mutant enzyme Q47E
7286
NADP+
pH 8.0, 30°C, recombinant enzyme
7364
NADP+
-
25°C, pH 7.8, mutant enzyme T14A
15500
NADP+
-
25°C, pH 7.8, mutant enzyme K343Q
18870
NADP+
-
25°C, pH 7.8, mutant enzyme Y179F
27050
NADP+
-
25°C, pH 7.8, mutant enzyme T14S
29230
NADP+
-
25°C, pH 7.8, mutant enzyme Y415F
31400
NADP+
-
25°C, pH 7.8, mutant enzyme Q47A
33900
NADP+
-
25°C, pH 7.8, mutant enzyme K343R
39080
NADP+
-
25°C, pH 7.8, mutant enzyme K182R
46760
NADP+
-
25°C, pH 7.8, mutant enzyme K182Q
65250
NADP+
25°C, pH 7.6, wild-type enzyme
65330
NADP+
-
wild type enzyme, in 33 mM Tris-HCl, pH 7.6, at 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.12
2',5'-ADP
-
pH 7.8, 25°C, substrate: NADP+
1.3
2'-AMP
-
pH 7.8, 25°C, substrate: NAD+
2
5'-AMP
-
pH 7.8, 25°C, substrate: NAD+
1
acetyl-CoA
-
24°C, pH 7.8, inhibition of NAD+-dependent reaction
36
adenosine
-
pH 7.8, 25°C, substrate: NAD+
3.1
ADP
-
pH 7.8, 25°C, substrate: NAD+
0.52
ADP-ribose
-
pH 7.8, 25°C, substrate: NAD+
0.15
cis-9-octadecenoyl-CoA
-
24°C, pH 7.8, inhibition of NAD+-dependent reaction
0.7
CoA
-
24°C, pH 7.8, inhibition of NAD+-dependent reaction
0.4
malonyl-CoA
-
24°C, pH 7.8, inhibition of NAD+-dependent reaction
95
N'-methylnicotinamide
-
pH 7.8, 25°C, substrate: NAD+
1.8
NADP+ 2',3'-dialdehyde
-
25°C, pH 7.8
105
nicotinamide
-
pH 7.8, 25°C, substrate: NAD+
0.034 - 0.04
pyridoxal 5'-diphospho-5'-adenosine
0.039
pyridoxal 5'-phosphate
-
25°C, pH 7.7, competitive inhibition when glucose 6-phosphate is varied at a constant, nearly saturating concentration of NAD+
additional information
vanadate
-
inhibition constants with respect to D-glucose 6-phosphate, NAD+ or NADP+
0.3
ATP
pH 8.0, 30°C
0.5
ATP
-
24°C, pH 7.8, inhibition of NAD+-dependent reaction
1.5
ATP
-
pH 7.8, 25°C, substrate: NADP+
0.76
NAD+
-
25°C, pH 7.8
1.148
NAD+
pH 8.0, 30°C, recombinant enzyme
1.148
NAD+
-
at pH 8.0 and 30°C
0.00337
NADP+
-
wild type enzyme, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.0034
NADP+
25°C, pH 7.6, wild-type enzyme
0.0037
NADP+
-
25°C, pH 6.7
0.0037
NADP+
-
25°C, pH 7.6, mutant enzyme H1787N
0.0039
NADP+
-
25°C, pH 6.2
0.005
NADP+
-
25°C, pH 7.2
0.0062
NADP+
25°C, pH 7.6, wild-type enzyme, mutant enzyme K121R
0.0067
NADP+
-
25°C, pH 7.8, mutant enzyme K343R
0.0073
NADP+
-
25°C, pH 7.8, mutant enzyme Y179F
0.0078
NADP+
25°C, pH 7.6, wild-type enzyme, mutant enzyme K21Q
0.0078
NADP+
-
25°C, pH 7.8, mutant enzyme K182Q
0.0079
NADP+
-
25°C, pH 7.8, mutant enzyme D374Q
0.008
NADP+
-
25°C, pH 7.8, mutant enzyme K182R
0.015
NADP+
-
25°C, pH 7.6, mutant enzyme D177N
0.016
NADP+
-
25°C, pH 7.8, mutant enzyme T14S
0.017
NADP+
-
25°C, pH 7.8, mutant enzyme Y415F
0.019
NADP+
-
25°C, pH 7.8, mutant enzyme P149G
0.034
NADP+
-
25°C, pH 7.8, mutant enzyme P149V
0.087
NADP+
-
25°C, pH 7.8, mutant enzyme Q47E
0.111
NADP+
pH 8.0, 30°C, recombinant enzyme
0.111
NADP+
-
at pH 8.0 and 30°C
0.169
NADP+
-
25°C, pH 7.8, mutant enzyme T14A
1.79
NADP+
-
mutant enzyme R46Q, in 33 mM Tris-HCl, pH 7.6, at 25°C
1.8
NADP+
-
25°C, pH 7.6, mutant enzyme R46Q
8.23
NADP+
-
25°C, pH 7.6, mutant enzyme R46A
8.23
NADP+
-
mutant enzyme R46A, in 33 mM Tris-HCl, pH 7.6, at 25°C
0.006
NADPH
-
25°C, pH 6.2
0.035 - 0.163
NADPH
pH 8.0, 30°C, recombinant enzyme
0.038
NADPH
-
25°C, pH 7.2
0.034
pyridoxal 5'-diphospho-5'-adenosine
-
25°C, pH 7.8, NAD+-linked reaction
0.04
pyridoxal 5'-diphospho-5'-adenosine
-
25°C, pH 7.8, NADP+-linked reaction
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.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D205C
-
enzyme variant with cysteine close to the dimer interface, about 30% loss of specific activity compared to wild-type enzyme shows changes in activity and the efficacy of immobilization.
D374Q
-
kcat/Km for D-glucose 6-phosphate is 7.7fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 7.3fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 12.2fold lower compared to kcat/KM of wild-type enzyme
D453C
-
enzyme variant with cysteine far from the active center, no significant loss in specific activity compared to wild-type enzyme, in contrast to wild-type enzyme, the mutant enzyme is readily immobilited
H178N
-
kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme
H250N
-
kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme
K182Q
-
kcat/Km for D-glucose 6-phosphate is 127fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.1fold higher compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.4fold lower compared to kcat/KM of wild-type enzyme
K182R
-
kcat/Km for D-glucose 6-phosphate is 81fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.1fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.6fold lower compared to kcat/KM of wild-type enzyme
K21Q
kcat/Km for D-glucose 6-phosphate in the NADP+-dependent reaction is 76.2fold lower compared to wild-type value, kcat/Km for D-glucose 6-phosphate in the NAD+-dependent reaction is 28.5fold lower compared to wild-type value
K21R
kcat/Km for D-glucose 6-phosphate in the NADP+-dependent reaction is 1.9fold lower compared to wild-type value, kcat/Km for D-glucose 6-phosphate in the NAD+-dependent reaction is 1.4fold lower compared to wild-type value
K343Q
-
kcat/Km for D-glucose 6-phosphate is 445fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 2.7fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 2.6fold lower compared to kcat/KM of wild-type enzyme
K343R
-
kcat/Km for D-glucose 6-phosphate is 23fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.2fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 2fold lower compared to kcat/KM of wild-type enzyme
L218C
-
enzyme variant with cysteine close to the active center, about 30% loss of specific activity compared to wild-type enzyme, the mutant enzyme shows almost complete immobilization but poor carrier activity
P149G
-
kcat/Km for D-glucose 6-phosphate is 890fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 120fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 448fold lower compared to kcat/KM of wild-type enzyme
P149V
-
kcat/Km for D-glucose 6-phosphate is 5933fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1265fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 3843fold lower compared to kcat/KM of wild-type enzyme
Q47A
-
kcat/Km for D-glucose 6-phosphate is 1.1fold higher compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.3fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.8fold lower compared to kcat/KM of wild-type enzyme
Q47E
-
kcat/Km for D-glucose 6-phosphate is 1.3fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 6.4fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.7fold lower compared to kcat/KM of wild-type enzyme
R46C
-
mutant glucose-6-phosphate dehydrogenases with coenzyme specificity that favors NAD+, whereas the wild-type enzyme prefers NADP+ as coenzyme
R46E
-
kcat/Km for D-glucose 6-phosphate is 4.8fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1406fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 6.7fold lower compared to kcat/KM of wild-type enzyme
R46Q
-
the enzyme's Km and Ki values for NADP+ are greatly increased (2-3 orders of magnitude)
T14A
-
kcat/Km for D-glucose 6-phosphate is 1.8fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 5.7fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 12.8fold lower compared to kcat/KM of wild-type enzyme
T14S
-
kcat/Km for D-glucose 6-phosphate is 1.1fold higher compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.6fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.5fold lower compared to kcat/KM of wild-type enzyme
Y179F
-
kcat/Km for D-glucose 6-phosphate is 4.9fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 2.2fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.7fold lower compared to kcat/KM of wild-type enzyme
Y415F
-
kcat/Km for D-glucose 6-phosphate is 1.2fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NADP+ is 1.4fold lower compared to kcat/KM of wild-type enzyme, kcat/Km for NAD+ is 1.6fold lower compared to kcat/KM of wild-type enzyme
D177N
absence of a negatively charged aspartate at 177 accounts for the decrease in catalytic activity at pH 7.8
D177N
-
kcat/KM for D-glucose 6-phosphate (with cosubstrate NADP+) is fold lower than the value for the wild-type enzyme, kcat/KM for NADP+ is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD) is fold lower than the value for the wild-type enzyme, kcat/KM for D-glucose 6-phosphate (with cosubstrate NAD+) is fold lower than the value for the wild-type enzyme
R46A
-
mutant glucose-6-phosphate dehydrogenases with coenzyme specificity that favors NAD+, whereas the wild-type enzyme prefers NADP+ as coenzyme
R46A
-
the enzyme's Km and Ki values for NADP+ are greatly increased (2-3 orders of magnitude)
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.
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.
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.
Naylor, C.E., Gover, S.; Basak, A.K.; Cosgrove, M.S.; Levy, H.R.; Adams, M.J.
NADP+ and NAD+ binding to the dual coenzyme specific enzyme Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different interdomain hinge angles are seen in different binary and ternary complexes
Acta Crystallogr. Sect. D
57
635-648
2001
Leuconostoc mesenteroides (P11411)
brenda
Grove, T.H.; Ishaque, A.; Levy, H.R.
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Interaction of the enzyme with coenzymes and coenzyme analogs
Arch. Biochem. Biophys.
17
307-316
1976
Leuconostoc mesenteroides
brenda
Levy, H.R.; Daouk, G.H.; Katopes, M.A.
Regulation of coenzyme utilization by the dual nucleotide-specific glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroids
Arch. Biochem. Biophys.
198
406-413
1979
Leuconostoc mesenteroides
brenda
Levy, H.R.; Christoff, M.; Ingulli, J.; Ho, E.M.
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: revised kinetic mechanism and kinetics of ATP inhibition
Arch. Biochem. Biophys.
222
473-488
1983
Leuconostoc mesenteroides
brenda
Kurlandsky, S.B.; Hilburger, A.C.; Levy, H.R.
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: ligand-induced conformational changes
Arch. Biochem. Biophys.
264
93-102
1988
Leuconostoc mesenteroides
brenda
Szweda, L.I.; Stadtman, E.R.
Oxidative modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides by an iron(II)-citrate complex
Arch. Biochem. Biophys.
301
391-395
1993
Leuconostoc mesenteroides
brenda
Levy, H.R.; Vought, V.E.; Yin, X.; Adams, M.J.
Identification of an arginine residue in the dual coenzyme-specific glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides that plays a key role in binding NADP+ but not NAD+
Arch. Biochem. Biophys.
326
145-151
1996
Leuconostoc mesenteroides
brenda
Coe, E.L.; Hsu, L.H.
Acyl coenzyme A inhibition of Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase: a comparison of the TPN and DPN linked reactions
Biochem. Biophys. Res. Commun.
53
66-69
1973
Leuconostoc mesenteroides
brenda
Haghighi, B.; Levy, H.R.
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Conformational transitions induced by nicotinamide adenine dinucleotide, nicotinamide adenine dinucleotide phosphate, and glucose 6-phosphate monitored by fluorescent probes
Biochemistry
21
6421-6428
1982
Leuconostoc mesenteroides
brenda
Haghighi, B.; Levy, H.R.
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetics of reassociation and reactivation from inactive subunits
Biochemistry
21
6429-6434
1982
Leuconostoc mesenteroides
brenda
Crans, D.C., Schelble, S.M.
Vanadate dimer and tetramer both inhibit glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides
Biochemistry
29
6698-6706
1990
Leuconostoc mesenteroides
brenda
Cosgrove, M.S.; Naylor, C.; Paludan, S.; Adams, M.J.; Levy, H.R.
On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase
Biochemistry
37
2759-2767
1998
Leuconostoc mesenteroides
brenda
Cosgrove, M.S.; Gover, S.; Naylor, C.E.; Vandeputte-Rutten, L.; Adams, M.J.; Levy, H.R.
An examination of the role of asp-177 in the His-Asp catalytic dyad of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray structure and pH dependence of kinetic parameters of the D177N mutant enzyme
Biochemistry
39
15002-15011
2000
Leuconostoc mesenteroides (P11411)
brenda
Vought, V.; Ciccone, T.; Davino, M.H.; Fairbairn, L.; Lin, Y.; Cosgrove, M.S.; Adams, M.J.; Levy, H.R.
Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase
Biochemistry
39
15012-15021
2000
Leuconostoc mesenteroides
brenda
Plomer, J.J.; Gafni, A.
Denaturation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides by guanidine hydrochloride; identification of inactive, partially unfolded, dimeric intermediates
Biochim. Biophys. Acta
1122
234-242
1992
Leuconostoc mesenteroides
brenda
Plomer, J.J.; Gafni, A.
Renaturation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides after denaturation in 4 M guanidine hydrochloride: kinetics of aggregation and reactivation
Biochim. Biophys. Acta
1163
89-96
1993
Leuconostoc mesenteroides
brenda
Murphy, N.B.; McConnell, D.J.; Schwarz, T.F.
Expression of the gene for NAD-dependent glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides cloned in Escherichia coli K-12
J. Bacteriol.
169
334-339
1987
Leuconostoc mesenteroides
brenda
Olive, C.; Geroch, M.E.; Levy, H.R.
Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetic studies
J. Biol. Chem.
246
2047-2057
1971
Leuconostoc mesenteroides
brenda
Levy, H.R.; Daouk, G.H.
Simultaneous analysis of NAD- and NADP-linked activities of dual nucleotide-specific dehydrogenases. Application to Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase
J. Biol. Chem.
254
4843-4837
1997
Leuconostoc mesenteroides
brenda
Adams, M.J.; Levy, H.R.; Moffat, K.
Crystallization and preliminary x-ray data for glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides
J. Biol. Chem.
258
5867-5868
1983
Leuconostoc mesenteroides
brenda
White, B.J.; Levy, H.R.
Modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides with the 2',3'-dialdehyde derivative of NADP+ (oNADP+)
J. Biol. Chem.
262
1223-1229
1987
Leuconostoc mesenteroides
brenda
Lee, W.T.; Flynn, T.G.; Lyons, C.; Levy, H.R.
Cloning of the gene and amino acid sequence for glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides
J. Biol. Chem.
266
13028-13034
1991
Leuconostoc mesenteroides (P11411), Leuconostoc mesenteroides
brenda
LaDine, J.R.; Carlow, D.; Lee, W.T.; Cross, R.L.; Flynn, T.G.; Levy, H.R.
Interaction of Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase with pyridoxal 5'-diphospho-5'-adenosine. Affinity labeling of Lys-21 and Lys-343
J. Biol. Chem.
266
5558-5562
1991
Leuconostoc mesenteroides
brenda
Szweda, L.I.; Stadtman, E.R.
Iron-catalyzed oxidative modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Structural and functional changes
J. Biol. Chem.
267
3096-3100
1992
Leuconostoc mesenteroides
brenda
Szweda, L.I.; Uchida, K.; Tsai, L.; Stadtman, E.R.
Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Selective modification of an active-site lysine
J. Biol. Chem.
268
3342-3347
1993
Leuconostoc mesenteroides
brenda
Simons, J.R.; Mosisch, M.; Torda, A.E.; Hilterhaus, L.
Site directed immobilization of glucose-6-phosphate dehydrogenase via thiol-disulfide interchange: influence on catalytic activity of cysteines introduced at different positions
J. Biotechnol.
167
1-7
2013
Leuconostoc mesenteroides
brenda
Ravera, S.; Calzia, D.; Morelli, A.; Panfoli, I.
Oligomerization studies of Leuconostoc mesenteroides G6PD activity after SDS-PAGE and blotting
Mol. Biol.
44
472-476
2010
Leuconostoc mesenteroides
brenda
Lee, W.T.; Levy, H.R.
Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction
Protein Sci.
1
329-334
1992
Leuconostoc mesenteroides (P11411)
brenda
Adams, M.J.; Basak, A.K.; Gover, S.; Rowland, P.; Levy, H.R.
Site-directed mutagenesis to facilitate X-ray structural studies of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase
Protein Sci.
2
859-662
1993
Leuconostoc mesenteroides (P11411)
brenda
Yamashiro, T.; Murata, K.; Kawai, S.
Extremely high intracellular concentration of glucose-6-phosphate and NAD(H) in Deinococcus radiodurans
Extremophiles
21
399-407
2017
Deinococcus radiodurans, Deinococcus radiodurans MK5205
brenda
Olavarria, K.; Marone, M.P.; da Costa Oliveira, H.; Roncallo, J.C.; da Costa Vasconcelos, F.N.; da Silva, L.F.; Gomez, J.G.
Quantifying NAD(P)H production in the upper Entner-Doudoroff pathway from Pseudomonas putida KT2440
FEBS Open Bio
5
908-915
2015
Pseudomonas putida, Pseudomonas putida KT 2240
brenda
Cumana, S.; Simons, J.; Liese, A.; Hilterhaus, L.; Smirnova, I.
Immobilization of glucose 6-phosphate dehydrogenase in silica-based hydrogels: A comparative study
J. Mol. Catal. B
85-86
220-228
2013
Leuconostoc mesenteroides
-
brenda
Olavarria, K.; Marone, M.P.; da Costa Oliveira, H.; Roncallo, J.C.; da Costa Vasconcelos, F.N.; da Silva, L.F.; Gomez, J.G.
Quantifying NAD(P)H production in the upper Entner-Doudoroff pathway from Pseudomonas putida KT2440
FEBS open bio
5
908-915
2015
Pseudomonas putida (A0A1B2F298), Pseudomonas putida KT 2240 (A0A1B2F298)
brenda
Zhu, S.; Cai, D.; Liu, Z.; Zhang, B.; Li, J.; Chen, S.; Ma, X.
Enhancement of bacitracin production by NADPH generation via overexpressing glucose-6-phosphate dehydrogenase Zwf in Bacillus licheniformis
Appl. Biochem. Biotechnol.
187
1502-1514
2019
Bacillus licheniformis, Bacillus licheniformis DW2
brenda
Benitez-Rangel, E.; Rodriguez-Hernandez, A.; Velasco-Garcia, R.
The substrate of the glucose-6-phosphate dehydrogenase of Pseudomonas aeruginosa provides structural stability
Biochim. Biophys. Acta Proteins Proteom.
1868
140331
2020
Pseudomonas aeruginosa
brenda
TranNgoc, K.; Pham, N.; Lee, C.; Jang, S.H.
Cloning, expression, and characterization of a psychrophilic glucose 6-phosphate dehydrogenase from Sphingomonas sp. PAMC 26621
Int. J. Mol. Sci.
20
1362
2019
Sphingomonas sp. PAMC 26621
brenda
Acero-Navarro, K.E.; Jimenez-Ramirez, M.; Villalobos, M.A.; Vargas-Martinez, R.; Perales-Vela, H.V.; Velasco-Garcia, R.
Cloning, overexpression, and purification of glucose-6-phosphate dehydrogenase of Pseudomonas aeruginosa
Protein Expr. Purif.
142
53-61
2018
Pseudomonas aeruginosa (O68282), Pseudomonas aeruginosa, Pseudomonas aeruginosa ATCC 15692 (O68282)
brenda