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Literature summary for 5.4.2.12 extracted from

  • Kuhn, N.J.; Setlow, B.; Setlow, P.
    Manganese(II) activation of 3-phosphoglycerate mutase of Bacillus megaterium: pH-sensitive interconversion of active and inactive forms (1993), Arch. Biochem. Biophys., 306, 342-349.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
EDTA complete inactivation, reactivation by Mn2+ Priestia megaterium

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ specific activator, none of the metal ions tested reaches more than 4% of the activity of EDTA-treated enzyme reactivated with Mn2+. Activation by Mn2+ is strongly pH-dependent within the physiological range Priestia megaterium
additional information Cd2+, Zn2+, Fe2+, Ni2+, Cu2+, Mg2+, Ca2+, Sr2+, or Ba2+ give no more than 4% of the activity of EDTA-treated enzyme reactivated with Mn2+ Priestia megaterium

Organism

Organism UniProt Comment Textmining
Priestia megaterium
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
reactivation of EDTA-treated enzyme by Mn2+. Several activation-deactivation cycles can be elicited Priestia megaterium