G5885
Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides
lyophilized powder, >= 550 units/mg protein (biuret)
Synonym(s):
G-6-P-DH
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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-602-6
MDL number:
Specific activity:
>= 550 units/mg protein (biuret)
Biological source:
bacterial (Leuconostoc mesenteroides)
biological source
bacterial (Leuconostoc mesenteroides)
Quality Level
type
Type XXIV
form
lyophilized powder
specific activity
>= 550 units/mg protein (biuret)
mol wt
128 kDa
composition
Protein, 15-40% biuret
application(s)
agriculture
foreign activity
6-Phosphogluconic dehydrogenase, hexokinase, NADH oxidase and NADPH oxidase ≤0.005%, PGI ≤0.01%
storage temp.
2-8°C
General description
Glucose-6-Phophate Dehydrogenase (G-6-PDH) comprises His-Asp catalytic dyad and exists as a homodimer. Structurally, G-6-PDH encompasses a Rossmann dinucleotide binding fold in the coenzyme binding domain region. It also harbors a large β + α domain and has a unique aspartate residue at position 374.
Application
Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides has been used along with hexokinase in the determination of glucose from mice liver samples.
Biochem/physiol Actions
Glucose-6-Phophate Dehydrogenase (G-6-PDH) can utilize either nicotinamide adenine dinucleotide phosphate (NADP+) or NAD+ as coenzyme making it crucial for bacterial metabolism.
Glucose-6-phosphate dehydrogenase (G6PD) catalyzes the conversion of glucose-6-phosphate to 6-phosphogluconolacetone as the first step in the pentose phosphate pathway.
Physical form
Lyophilized powder containing Ficoll and Tris buffer salts
Other Notes
One unit will oxidize 1.0 μmole of D-glucose 6-phosphate to 6-phospho-D-gluconate per min in the presence of NAD at pH 7.8 at 30 °C.
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Related Content
Product Information Sheet
V Vought et al.
Biochemistry, 39(49), 15012-15021 (2000-12-07)
The roles of particular amino acids in substrate and coenzyme binding and catalysis of glucose-6-phosphate dehydrogenase of Leuconostoc mesenteroides have been investigated by site-directed mutagenesis, kinetic analysis, and determination of binding constants. The enzyme from this species has functional dual
M S Cosgrove et al.
Biochemistry, 39(49), 15002-15011 (2000-12-07)
The role of Asp-177 in the His-Asp catalytic dyad of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides has been investigated by a structural and functional characterization of the D177N mutant enzyme. Its three-dimensional structure has been determined by X-ray cryocrystallography in
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