G5885
Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides
lyophilized powder, >= 550 units/mg protein (biuret)
Synonyme(s) :
G-6-P-DH
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A propos de cet article
Numéro CAS:
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)
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Laissez-nous vous aiderbiological source
bacterial (Leuconostoc mesenteroides)
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
Quality Level
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Catégories apparentées
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Classe de stockage
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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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
J Pozueta-Romero et al.
FEBS letters, 291(2), 233-237 (1991-10-21)
The standardized enzyme coupling method for assaying sucrose synthase activities in the direction of sucrose cleavage was reexamined using enzyme preparations from cultured cells of sycamore (Acer pseudoplatanus L.) and spinach leaves (Spinacea oleracea). Both ATP and Tris, commonly utilized
Hana A Dibe et al.
Physiological reports, 8(3), e14370-e14370 (2020-02-16)
The liver is the primary metabolic organ involved in the endogenous production of glucose through glycogenolysis and gluconeogenesis. Hepatic glucose production (HGP) is increased via neural-hormonal mechanisms such as increases in catecholamines. To date, the effects of prior exercise training
Enzyme-stabilizing activity of seed trypsin inhibitors during desiccation
Ji-Ming Lam, Keng-Hock Pwee, Wendell Q. Sun, Yii-Leng Chua, Xing-Jun Wang
Plant Science, 142, 209-218 (1999)
Contenu apparenté
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