Literature summary for 1.1.1.363 extracted from

Haghighi, B.; Levy, H.R.
Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Kinetics of reassociation and reactivation from inactive subunits (1982), Biochemistry, 21, 6429-6434.

Search for more literature for 1.1.1.363

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.0047	-	NADP+	25°C, pH 7.8	Leuconostoc mesenteroides
0.078	-	D-glucose 6-phosphate	25°C, pH 7.8, NAD+-dependent reaction	Leuconostoc mesenteroides
0.09	-	D-glucose 6-phosphate	25°C, pH 7.8, NADP+-dependent reaction	Leuconostoc mesenteroides
0.102	-	NAD+	25°C, pH 7.8	Leuconostoc mesenteroides

Organism

Organism	UniProt	Comment	Textmining
Leuconostoc mesenteroides	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
denatured in 8 M urea and dissociated into its two inactive subunits (MW 50000 Da). Denaturation leads to an approximately 80% decrease in protein fluorescence and a 20-nm red shift in the emission maximum. Upon dilution, the urea-treated enzyme regains catalytic activity (approximately 70%). The reactivated enzyme is indistinguishable from the native enzyme based on a number of physicochemical and enzymological criteria. The kinetics of renaturation and reactivation are monitored. Reactivation is stimulated to different degrees by either the initial or delayed addition of NAD+, NADP+, or glucose 6-phosphate. During the initial, rapid phase of renaturation, approximately 3 of the enzyme's 12 histidine residues become unreactive toward diethyl pyrocarbonate; concomitant with the subsequent reactivation, approximately 7 more histidines become inaccessible to diethyl pyrocarbonate	Leuconostoc mesenteroides

Renatured (Comment)

Organism

denatured in 8 M urea and dissociated into its two inactive subunits (MW 50000 Da). Denaturation leads to an approximately 80% decrease in protein fluorescence and a 20-nm red shift in the emission maximum. Upon dilution, the urea-treated enzyme regains catalytic activity (approximately 70%). The reactivated enzyme is indistinguishable from the native enzyme based on a number of physicochemical and enzymological criteria. The kinetics of renaturation and reactivation are monitored. Reactivation is stimulated to different degrees by either the initial or delayed addition of NAD+, NADP+, or glucose 6-phosphate. During the initial, rapid phase of renaturation, approximately 3 of the enzyme's 12 histidine residues become unreactive toward diethyl pyrocarbonate; concomitant with the subsequent reactivation, approximately 7 more histidines become inaccessible to diethyl pyrocarbonate

Leuconostoc mesenteroides

Substrates and Products (Substrate)

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