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.

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

     1 Oxidoreductases

         1.1 Acting on the CH-OH group of donors

             1.1.1 With NAD⁺ or NADP⁺ as acceptor

                1.1.1.363 glucose-6-phosphate dehydrogenase [NAD(P)+]

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Results	in table
2	Activating Compound
56	AA Sequence
2	Application
10	Cloned(Commentary)
38	Cofactor
5	Crystallization (Commentary)
5	General Information
8	General Stability
1	IC50 Value
57	Inhibitors
102	kcat/KM [mM/s]
54	Ki Value [mM]
154	KM Value [mM]
2	Metals/Ions
6	Molecular Weight [Da]
38	Natural Substrates/ Products (Substrates)
3	Organic Solvent Stability
82	Organism
6	Pathway
9	pH Optimum
1	pH Range
1	pI Value
27	Protein Variants
9	Purification (Commentary)
4	Reaction
42	Reference
2	Renatured (Commentary)
10	Specific Activity [micromol/min/mg]
1	Storage Stability
75	Substrates and Products (Substrate)
5	Subunits
36	Synonyms
1	Systematic Name
11	Temperature Optimum [°C]
4	Temperature Stability [°C]
104	Turnover Number [1/s]

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RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

denatured in 8 M urea and dissociated into its two inactive subunits (MW 50000 Da). Denaturation leads to an approximately 80% decrease in protein fluorescence and a 20-nm red shift in the emission maximum. Upon dilution, the urea-treated enzyme regains catalytic activity (approximately 70%). The reactivated enzyme is indistinguishable from the native enzyme based on a number of physicochemical and enzymological criteria. The kinetics of renaturation and reactivation are monitored. Reactivation is stimulated to different degrees by either the initial or delayed addition of NAD+, NADP+, or glucose 6-phosphate. During the initial, rapid phase of renaturation, approximately 3 of the enzyme's 12 histidine residues become unreactive toward diethyl pyrocarbonate; concomitant with the subsequent reactivation, approximately 7 more histidines become inaccessible to diethyl pyrocarbonate

Leuconostoc mesenteroides

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721570

in 4 M guanidine-HCl, the dimeric enzyme glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides dissociates to subunits and is extensively unfolded. Rapid dilution of this high guanidine hydrochloride concentration allowes the enzyme to partially renature. The fraction of the enzyme which does not renature aggregates and precipitates out of solution, a process which can not be substantially prevented by stabilizing additives. A renaturation mechanism is described, which involves a bi-unimolecular (subunit association-folding) reaction sequence. This mechanism involves an inactive, dimeric, glucose-6-phosphate dehydrogenase-folding intermediate

Leuconostoc mesenteroides

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721695