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Literature summary for 1.1.1.49 extracted from

  • Sanwal, B.D.
    Regulatory mechanisms involving nicotinamide adenine nucleotides as allosteric effectors. 3. Control of glucose 6-phosphate dehydrogenase (1970), J. Biol. Chem., 245, 1626-1631.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
spermidine activation constant: 0.2 mM Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
NADH allosteric inhibition, inhibition is not reversed by NAD+, AMP, or spermidine Escherichia coli
NADPH when NADP+ is the varied substrate, NADPH NADPH is a competitive inhibitor both in the presence and absence of Mg2+, linear competitive inhibition. When glucose 6-phosphate is the varied substrate NADPH causes linear noncompetitive inhibition Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information the initial velocity plots of the enzyme follow the Michaelis-Menten equation in the absence of NADH. In its presence, however, the velocity versus substrate plots for NADP+ become sigmoidal but remain hyperbolic for glucose 6-phosphate as the variable substrate. Inhibition against both of the substrates of the enzyme by NADH is noncompetitive. The inhibition curves for NADH are also sigmoidal, suggesting a multisite binding of the inhibitor on the enzyme surface Escherichia coli
0.015
-
NADP+ pH 8.0, temperature not specified in the publication Escherichia coli
0.07
-
D-glucose 6-phosphate pH 8.0, temperature not specified in the publication Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates, no absolute requirement. In the presence of saturating concentrations of spermidine or other polycations, Mg2+ ions have no further stimulatory effect Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glucose 6-phosphate + NADP+ Escherichia coli oxidative pentose pathway 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose 6-phosphate + NADP+ Escherichia coli B / ATCC 11303 oxidative pentose pathway 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli B / ATCC 11303
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.7
-
pH 8.0, temperature not specified in the publication Escherichia coli

Storage Stability

Storage Stability Organism
-20°C, 0.05 M Tris-Cl buffer containing 1 mM glucose 6-phosphate, pH 7.5, stable for over 2 months Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose 6-phosphate + NADP+
-
Escherichia coli 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose 6-phosphate + NADP+ oxidative pentose pathway Escherichia coli 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose 6-phosphate + NADP+
-
Escherichia coli B / ATCC 11303 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose 6-phosphate + NADP+ oxidative pentose pathway Escherichia coli B / ATCC 11303 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADP+ almost specific for NADP+ as coenzyme. In presence of 2 and 3 mM NAD+ the velocity is about 2% compared to NADP+ Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.01
-
NADPH pH 8.0, temperature not specified in the publication, varied substrate: NADP+ Escherichia coli
0.04
-
NADPH pH 8.0, temperature not specified in the publication, varied substrate: glucose 6-phosphate, slope inhibition constant Escherichia coli
0.18
-
NADPH pH 8.0, temperature not specified in the publication, varied substrate: glucose 6-phosphate, intercept inhibition constant Escherichia coli