Structural Constraints of Possible Mechanisms of Lactate Dehydrogenase as Shown by High Resolution Studies of the Apoenzyme and a Variety of Enzyme Complexes

M.G. Rossmann, Margaret Adams, Manfred Buehner, Geoffrey C. Ford, Marvin L. Hackert, Alexander McPherson, Richard W. Schevitz, Ira E. Smiley

Cold Spring Harbor Symposia on Quantitative Biology · 1972 · 104 citations · 0 references

Concepts

Abstract

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).