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
Recommended Products
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
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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.
Unit Definition
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.
Physical form
Lyophilized powder containing Ficoll and Tris buffer salts
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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
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Protocols
Enzymatic Assay of Glucose-6-Phosphate Dehydrogenase (EC 1.1.1.49)
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