Substrate-dependent dissociation of malate thiokinase.

摘要: Malate thiokinase has been purified to apparent homogeneity by employing conventional purification techniques along with affinity chromatography. The enzyme is composed of two nonidentical subunits (alpha subunit Mr=34,000, beta Mr=42,500) yield an alpha 4 structure for the native enzyme. Phosphorylation ATP occurs exclusively on subunit. phosphorylated acid labile and base stable consistent phosphorylation a histidine residue. Dephosphorylation promoted ADP, succinate, malate, coenzyme A plus inorganic phosphate. leads reversible change in sedimentation properties enzyme; exhibits S20,w approximately 10, whereas phosphoenzyme 7. Formation 7 S form also observed when succinyl-CoA interact ratio both 10 forms 1.0, suggesting that 2 structure.