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Literature summary for 1.1.1.363 extracted from

  • 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 (1997), J. Biol. Chem., 254, 4843-4837.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ATP inhibits competitively with respect to thionicotinamide-NAD+ Leuconostoc mesenteroides
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+ Leuconostoc mesenteroides
NADH inhibits noncompetitively with respect to thionicotinamide-NAD+ Leuconostoc mesenteroides
NADPH inhibits competitively with respect to thionicotinamide-NADP+ Leuconostoc mesenteroides

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.001
-
thionicotinamide-NADP+ pH 7.8, 25°C Leuconostoc mesenteroides
0.006
-
NADP+ pH 7.8, 25°C Leuconostoc mesenteroides
0.007
-
D-glucose 6-phosphate pH 7.8, 25°C, cosubstrate: thionicotinamide-NAD+ Leuconostoc mesenteroides
0.009
-
D-glucose 6-phosphate pH 7.8, 25°C, cosubstrate: thionicotinamide-NADP+ Leuconostoc mesenteroides
0.011
-
thionicotinamide-NAD+ pH 7.8, 25°C Leuconostoc mesenteroides
0.053
-
D-glucose 6-phosphate pH 7.8, 25°C, cosubstrate: NAD+ Leuconostoc mesenteroides
0.081
-
D-glucose 6-phosphate pH 7.8, 25°C, cosubstrate: NADP+ Leuconostoc mesenteroides
0.106
-
NAD+ pH 7.8, 25°C Leuconostoc mesenteroides

Organism

Organism UniProt Comment Textmining
Leuconostoc mesenteroides
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
a method is described which enables one to assay simultaneously the NAD+- and NADP+-linked reactions of dehydrogenases which can utilize both coenzymes. The method is based on the fact that the thionicotinamide analogs of NADH and NADPH absorb light maximally at 400 nm, a wavelength sufficiently far removed from the absorbance maximum of NADH and NADPH to permit measurements of the simultaneous reduction of NAD+ (or NADP+) and the thionicotinamide analog of NADP+ (or NAD+). Application of the method to glucosed 6-phosphate dehydrogenase from Leuconostoc mesenteroides reveals differential effects of glucose 6-phosphate concentration on the NAD+- and NADP+-linked reactions catalyzed by this enzyme which can not be detected by conventional assay procedures and which may have regulatory significance Leuconostoc mesenteroides

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose 6-phosphate + NAD+ iso ordered bi bi reaction Leuconostoc mesenteroides 6-phospho-D-glucono-1,5-lactone + NADH + H+
-
?
D-glucose 6-phosphate + NADP+ ordered bi bi reaction Leuconostoc mesenteroides 6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
?
D-glucose 6-phosphate + thionicotinamide-NAD+
-
Leuconostoc mesenteroides 6-phospho-D-glucono-1,5-lactone + thionicotinamide-NADH + H+
-
?
D-glucose 6-phosphate + thionicotinamide-NADP+
-
Leuconostoc mesenteroides 6-phospho-D-glucono-1,5-lactone + thionicotinamide-NADPH + H+
-
?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Leuconostoc mesenteroides
NADP+
-
Leuconostoc mesenteroides