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

BRENDA support

Literature summary for 1.1.1.49 extracted from

  • Holmes, P.K.; Levinson, H.S.
    Thermal stimulation of Bacillus megaterium glucose-6-phosphate dehydrogenase (1970), Biochem. Biophys. Res. Commun., 38, 143-148.
    View publication on PubMed
Search for more literature for 1.1.1.49

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibited by ATP, phosphate, or Mg2+ Priestia megaterium

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ is markedly stimulated by (but not absolutely dependent upon) Mg2+ Priestia megaterium
Mn2+ is markedly stimulated by (but not absolutely dependent upon) Mn2+ Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-
Priestia megaterium QM Bl551
-
-
-

Synonyms

Synonyms Comment Organism
D-glucose-6-phosphate:NADP oxidoreductase
-
 Priestia megaterium
NADP-glucose-6-phosphate dehydrogenase
-
 Priestia megaterium

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
-
 30 activity is increased 2-3fold by heating at 25°C (either at pH 10 in 0.5 M glycine KOH buffer or at pH 5 in 0.05 M sodium citrate buffer) prior to assay, the stimulation is reversed by chilling to 0°C but is not reversed at temperatures between 20°C and 30°C Priestia megaterium

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 in 0.05 M sodium citrate buffer Priestia megaterium
10
-
 in 0.5 M glycine-KOH buffer Priestia megaterium

pH Stability

pH Stability pH Stability Maximum Comment Organism
8 10.5 the enzyme displays a peak of activity at pH 10 in glycine-KOH buffer and is half-maximally active in this buffer at pH 8 and at pH 10.5 Priestia megaterium

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Priestia megaterium