1.1.1.363: glucose-6-phosphate dehydrogenase [NAD(P)+]
This is an abbreviated version!
For detailed information about glucose-6-phosphate dehydrogenase [NAD(P)+], go to the full flat file.
Word Map on EC 1.1.1.363
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1.1.1.363
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citrate
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mesenteroides
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leuconostoc
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clarias
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batrachus
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4-hydroxy-2-nonenal
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freshwater
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multicatalytic
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catfish
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hne
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hne-treated
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lipogenic
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8-anilino-1-naphthalenesulfonic
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actinomycin
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pentose
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disease-related
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teleost
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synthesis
- 1.1.1.363
- citrate
- mesenteroides
-
leuconostoc
-
clarias
- batrachus
- 4-hydroxy-2-nonenal
-
freshwater
-
multicatalytic
- catfish
- hne
-
hne-treated
-
lipogenic
-
8-anilino-1-naphthalenesulfonic
- actinomycin
- pentose
-
disease-related
-
teleost
- synthesis
Reaction
Synonyms
G6-PDH, G6PD, G6PDH, G6PDH-1, Glc6PD, Glu-6-PDH, glucose 6-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase Zwf, NADP+- and NAD+-dependent G6PDH, PputG6PDH-1, zwf-1
ECTree
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General Stability
General Stability on EC 1.1.1.363 - glucose-6-phosphate dehydrogenase [NAD(P)+]
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both after non-denaturing and after denaturing electrophoretic separation (SDS-PAGE) and blotting Leuconostoc mesenteroides G6PD retains its complete catalytic activity
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chymotrypsin inactivates. First order rate constant for inactivation is 0.02/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+
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eluted mutant enzyme D453C shows almost double the activity of the immobilized enzyme, which is consistent with 49% activity loss due to immobilization. Mutant enzyme D205C produces a 1.8-fold higher activity compared to its immobilized state. Eluted mutant enzyme L218C shows 9.9 times the activity of its immobilized state
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is the result of a structural change in the enzyme caused by glucose-6-phosphate dehydrogenase. In contrast to the human enzyme, the enzyme from Pseudomonas aeruginosa is not structurally stabilized by NADP+
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pronase inactivates. First order rate constant for inactivation is 0.012/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+
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the substrate glucose-6-phosphate stabilizes the enzyme and protects it from heat and urea denaturation. The stabilization
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thermolysin inactivates. First order rate constant for inactivation is 0.057/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+
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trypsin inactivates. First order rate constant for inactivation is 0.025/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+
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