Lactate dehydrogenase

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Lactate dehydrogenase M tetramer

Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). It catalyzes the conversion of lactate to pyruvic acid and back

This is an important function because lactic acid builds up in muscle tissue. LDH works to prevent muscle fatigue and failure in various ways.

Each LDH molecule is made of four subunits.[1] There are somewhat different types of LDH in different tissues. The main type in the lungs has two M subunits and two H subunits (2H2M). The M and H subunits are coded by two different genes. The M subunit is coded by LDHA on human chromosome 11, and the H subunit is coded by LDHB on chromosome 12.[2]

References[change | change source]

  1. Eventoff W. et al 1977. Structural adaptations of lactate dehydrogenase isozymes". Proceedings of the National Academy of Sciences of the United States of America. 74 (7): 2677–81. [1]
  2. Madern D. 2002. Molecular evolution within the L-malate and L-lactate dehydrogenase super-family. J Mol Evol. 54 (6): 825–40. [2]