G5885
Glucose-6-phosphate Dehydrogenase from Leuconostoc mesenteroides
lyophilized powder, >= 550 units/mg protein (biuret)
동의어(들):
G-6-P-DH
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
CAS 번호:
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)
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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관련 카테고리
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
저장 등급
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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
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)
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
A simple ultramicro method for determination of pyridine nucleotides in tissues.
J S Nisselbaum et al.
Analytical biochemistry, 27(2), 212-217 (1969-02-01)
Sofia Garcia et al.
Human molecular genetics, 31(5), 692-704 (2021-09-25)
We analyzed early brain metabolic adaptations in response to mitochondrial dysfunction in a mouse model of mitochondrial encephalopathy with complex IV deficiency [neuron-specific COX10 knockout (KO)]. In this mouse model, the onset of the mitochondrial defect did not coincide with
프로토콜
To measure glucose-6-phosphate dehydrogenase activity, beta-nicotinamide adenine dinucleotide phosphate is used in a spectrophotometric rate determination assay at 340 nm.
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