Literature summary for 1.1.1.49 extracted from

Verma, A.; Suthar, M.K.; Doharey, P.K.; Gupta, S.; Yadav, S.; Chauhan, P.M.; Saxena, J.K.
Molecular cloning and characterization of glucose-6-phosphate dehydrogenase from Brugia malayi (2013), Parasitology, 140, 897-906.

Search for more literature for 1.1.1.49

Activating Compound

Activating Compound	Comment	Organism	Structure
guanosine hydrochloride	the enzyme shows a sharp loss in activity above 0.75 M, but is activated by low concentrations of 0.2 M of GdmCl	Brugia malayi
N-ethylmaleimide	blocking the SH group leads to activation of rBmG6PD activity	Brugia malayi

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of His-tagged enzyme in Escherichia coli strain C41	Brugia malayi

General Stability

General Stability	Organism
unfolding equilibrium of rBmG6PD with GdmCl/urea shows the triphasic unfolding pattern along with the highly stable intermediate obtained by GdmCl	Brugia malayi

Inhibitors

Inhibitors	Comment	Organism	Structure
adenosine 5' [beta,gamma-amido] triphosphate	-	Brugia malayi
adenosine 5' [beta-thio] diphosphate	-	Brugia malayi
adenosine 5' [gamma-thio] triphosphate	-	Brugia malayi
ADP	15% inhibition at 2 mM	Brugia malayi
AMP	5% inhibition at 2 mM	Brugia malayi
ATP	31% inhibition at 5 mM, non-competitive inhibition with respect to D-glucose 6-phosphate	Brugia malayi
Cu2+	-	Brugia malayi
guanosine hydrochloride	the enzyme shows a sharp loss in activity above 0.75 M, but is activated by low concentrations of 0.2 M of GdmCl	Brugia malayi
K+	-	Brugia malayi
Li+	-	Brugia malayi
Na+	-	Brugia malayi
NADPH	competitive inhibition with respect to NADP+ and D-glucose 6-phosphate	Brugia malayi
phosphoenol pyruvate	25% inhibition at 10 mM	Brugia malayi
suramin	77% inhibition at 0.05 mM	Brugia malayi

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics	Brugia malayi

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Brugia malayi

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
75000	-	4 * 75000, recombinant His-tagged enzyme, SDS-PAGE	Brugia malayi
300000	-	recombinant His-tagged enzyme, gel filtration	Brugia malayi

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
D-glucose 6-phosphate + NADP+	Brugia malayi	-	D-glucono-1,5-lactone 6-phosphate + NADPH + H+	-	?

Organism

Organism	UniProt	Comment	Textmining
Brugia malayi	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain C41 by nickel affinity chromatography	Brugia malayi

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-glucose 6-phosphate + NADP+	-	Brugia malayi	D-glucono-1,5-lactone 6-phosphate + NADPH + H+	-	?

Subunits

Subunits	Comment	Organism
More	rBmG6PD is composed of 37% alpha-helices and 26% beta-sheets	Brugia malayi
tetramer	4 * 75000, recombinant His-tagged enzyme, SDS-PAGE	Brugia malayi

Synonyms

Synonyms	Comment	Organism
G6PD	-	Brugia malayi

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
40	-	-	Brugia malayi

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
50	-	purified recombinant His-tagged enzyme, inactivation	Brugia malayi

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
8.5	-	-	Brugia malayi

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Brugia malayi

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.025	-	NADPH	versus D-glucose 6-phosphate, pH 8.0, 25°C	Brugia malayi
0.04	-	NADPH	versus NADP+, pH 8.0, 25°C	Brugia malayi
6.5	-	ATP	pH 8.0, 25°C	Brugia malayi

General Information

General Information	Comment	Organism
metabolism	regulatory enzyme of the pentose phosphate pathway	Brugia malayi

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)