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Structural Constraints of Possible Mechanisms of Lactate Dehydrogenase as Shown by High Resolution Studies of the Apoenzyme and a Variety of Enzyme Complexes
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1972
Year
Molecular BiologySkeletal MuscleBioenergeticsM TypeStructural ConstraintsStructure-function Enzyme KineticsAlcohol DehydrogenasesM4 IsoenzymeHealth SciencesAnimal PhysiologyBiochemistryStructural BiologyEnergy MetabolismCellular EnzymologyEnzyme CatalysisLactate DehydrogenasePhysiologyEnzyme ComplexesMetabolismMedicine
In vertebrates, the NAD+-dependent enzyme lactate dehydrogenase (LDH) (EC 1.1.1.27) is a tetramer (mol wt 140,000) which catalyzes the interconversion of l(+) lactate and pyruvate. Two subunit types predominate, the M type in skeletal muscle and the H type in heart tissue. The subject of this study is the M4 isoenzyme from dogfish (Squalus acanthius).