Enzymatically active lactate dehydrogenase is consisting of four subunits (tetramer). The two most common subunits are the LDH-M and LDH-H peptides, named for their discovery in muscle and heart tissue, and encoded by the LDHA and LDHB genes, respectively. These two subunits can form five possible tetramers (isoenzymes): LDH-1 (4H), LDH-5 (4M), and the three mixed tetramers (LDH-2/3H1M, LDH-3/2H2M, LDH-4/1H3M). These five isoforms are enzymatically similar but show different tissue distribution.
* LDH-1 (4H)—in the heart and in RBC (red blood cells), as well as the brain
* LDH-2 (3H1M)—in the reticuloendothelial system
* LDH-3 (2H2M)—in the lungs
* LDH-4 (1H3M)—in the kidneys, placenta, and pancreas
* LDH-5 (4M)—in the liver and striated muscle, also present in the brain
LDH-2 is usually the predominant form in the serum. An LDH-1 level higher than the LDH-2 level (a "flipped pattern") suggests myocardial infarction (damage to heart tissues releases heart LDH, which is rich in LDH-1, into the bloodstream). The use of this phenomenon to diagnose infarction has been largely superseded by the use of Troponin I or T measurement.
There are two more mammalian LDH subunits that can be included in LDH tetramers: LDHC and LDHBx. LDHC is a testes-specific LDH protein, that is encoded by the LDHC gene. LDHBx is a peroxisome-specific LDH protein. LDHBx is the readthrough-form of LDHB. LDHBx is generated by translation of the LDHB mRNA, but the stop codon is interpreted as an amino acid-encoding codon. In consequence, translation continues to the next stop codon. This leads to the addition of seven amino acid residues to the normal LDH-H protein. The extension contains a peroxisomal targeting signal, so that LDHBx is imported into the peroxisome.