Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.49 extracted from

  • Hasmann, F.A.; Gurpilhares, D.B.; Roberto, I.C.; Converti, A.; Pessoa, A.
    New combined kinetic and thermodynamic approach to model glucose-6-phosphate dehydrogenase activity and stability (2007), Enzyme Microb. Technol., 40, 849-858.
No PubMed abstract available

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glucose-6-phosphate dehydrogenase from commercial Saccharomyces cerevisiae was concentrated by reverse micelles liquid-liquid extraction using soybean lecithin. Five successive cycles of extraction ensured a G6PD purification factor of 5.4. The kinetic and thermodynamic properties either of the concentrated fraction or the cell free extract are investigated. While the Michaelis constant for glucose-6-phosphate is almost independent of the presence of cell debris, the maximum initial activity is about 16% higher in its absence. The extraction seems to slightly improve both the enzyme activity and stability Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
G6PD
-
Saccharomyces cerevisiae

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
47
-
50 min, the enzyme is completely inactivated either in the cell free extract or in the concentrated fraction. The thermodynamic parameters of G6PD thermal inactivation suggests the occurrence of two inactivation events both related to breaking of bonds responsible for the active dimer integrity: one, prevailing at low temperature, likely led to the formation of a less active dimer, while the other, prevailing at high temperature, is responsible for the formation of a totally inactive dimer or monomer Saccharomyces cerevisiae