Succinate thiokinase in pigeon breast muscle mitochondria.
Succinate thiokinase has been purified from pigeon breast muscle. It has been confirmed that the enzyme is entirely specific for ATP, and Km is very high (approximately 0.8 mM). Activity in mitochondrial sonicates is low enough for it to be doubtful whether the enzyme can support citric acid cycle flux in the tissue. The enzyme appears to have an Mr of 80 000-100 000, and to have two unequal subunits. As determined by SDS gel electrophoresis one subunit certainly has an Mr of 40 000.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D003065:Coenzyme A / Q000378:metabolism; D003066:Coenzyme A Ligases / Q000302:isolation & purification*; D010856:Columbidae; D007700:Kinetics; D008931:Mitochondria, Muscle / Q000201:enzymology*; D013379:Substrate Specificity; D013389:Succinate-CoA Ligases / Q000302:isolation & purification* / Q000378:metabolism
D000255:Adenosine Triphosphate; D003066:Coenzyme A Ligases; D013389:Succinate-CoA Ligases; D003065:Coenzyme A