Pyruvate Kinase/Lactic Dehydrogenase enzymes from rabbit muscle has been used:
for ATP generation in the active microtubule preparation
in the enzyme linked ATPase assay of skeletal muscle heavy meromyosin (HMM)
as a standard control for quantifying mesenchymal stem cells (MSCs) lactate dehydrogenase
일반 설명
Pyruvate Kinase from rabbit muscle is a metalloenzyme which catalyzes the conversion of phosphoenol pyruvate to pyruvate in the glycolysis pathway. It corresponds to a molecular weight of 59 kDa. It exists as a tetramer and undergoes conformational changes in the active site to accommodate substrate. Lactic dehydrogenase (LDH) catalyzes the lactate to pyruvate conversion in anaerobic glycolysis. It exists as tetramer and comprises of two subunits (H and M). The LDH of eukaryotes undergo active-site loop gating for their catalytic functionality.
Biochem/physiol Actions
Pyruvate kinase requires bivalent and monovalent cations such as Mg2+ and K+ respectively for activation to occur.
