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]

Temperature Stability

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Temperature Stability on EC 1.1.1.363 - glucose-6-phosphate dehydrogenase [NAD(P)+]

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

4 - 20

Sphingomonas sp. PAMC 26621

-

the secondary structure of the enzyme is maintained between 4-40°C, its activity and tertiary structure are better preserved between 4-20°C

761295

49

Leuconostoc mesenteroides

-

first order rate constant for inactivation is 0.05/min. Protection by 72 mM NAD+ or by 6.3 mM glucose 6-phosphate or 72 mM NADP+

721406

60

Sphingomonas sp. PAMC 26621

-

20 min, complete loss of activity

761295

additional information

Leuconostoc mesenteroides

-

the enzyme is rapidly inactivated by micromolar concentrations of Fe2+ and H2O2. Fe2+ binds to the glucose 6-phosphate binding site and interaction of the enzyme-bound Fe2+ with H2O2 leads to the oxidative modification of amino acids essential for enzyme activity. Partially inactivated enzyme remains predominantly in the dimeric form, and no change in the apparent affinity of the remaining active subunits for substrate is observed. Partial inactivation leads to a decrease in the thermal stability of the remaining activity. This decrease in thermal stability could be largely overcome by the addition of glucose 6-phosphate. Thus, although exposure to H2O2 and Fe2+ results in the irreversible inactivation of the enzyme, the resulting modification is selective, leads to the formation of heterodimers of both active and inactive subunits, and does not appear to cause large scale structural changes

722593