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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Organic Solvent Stability
Organic Solvent Stability on EC 1.1.1.363 - glucose-6-phosphate dehydrogenase [NAD(P)+]
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guanidine-HCl
urea
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4 M. First order rate constant for inactivation is 0.019/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+
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between 0.9 and 1.2 M denaturant the enzyme undergoes a conformational change, exposing tryptophan residues to solvent, with some loss of secondary structure and a complete loss of enzymatic activity but without dimer dissociation to subunits. This inactive, partially unfolded, dimeric intermediate was susceptible to slow aggregation. A second equilibrium transition, reflecting extensive unfolding and dimer dissociation, occurrs at denaturant concentrations above 1.4 M. In the denaturant concentration range of 1.7-1.9 M the fluorescence change occurrs in two distinct steps. The first step involves a large, very rapid drop in fluorescence whose rate is strongly dependent on the denaturant concentration. This is followed by a small, relatively slow rise in the emission intensity, the rate of which is independent of denaturant concentration. Enzymatic activity is lost with a denaturant-concentration-dependent rate, which is approx. 3times slower than the rate of the first step in fluorescence change. A denaturation mechanism incorporating several unfolding intermediates and which accounts for all the above results is presented and discussed. While the fully unfolded enzyme regains up to 55% of its original activity upon dilution of denaturant to a concentration that would be expected to support native enzyme, denaturation intermediates are able to reactivate only minimally and in fact are found to aggregate and precipitate out of solution
guanidine-HCl
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in 4 M guanidine hydrochloride, the dimeric enzyme dissociates to subunits and is extensively unfolded