Lactate dehydrogenase

Lactate dehydrogenase (LDH or LD) is an <a href="/facts/Enzyme/DSI1Fh7y">enzyme</a> found in nearly all living cells. LDH catalyzes the conversion of <a href="/facts/Pyruvic_acid/qJTgl4J9">pyruvate</a> to <a href="/facts/Lactic_acid/BsVRFx7s">lactate</a> and back, as it converts NAD+ to <a href="/facts/NADH/BHdLW925">NADH</a> and back. A <a href="/facts/Dehydrogenase/hX7eulAz">dehydrogenase</a> is an enzyme that transfers a <a href="/facts/Hydride/v2rlBGMg">hydride</a> from one molecule to another. 
LDH exists in four distinct enzyme classes. This article is specifically about the <a href="/facts/NAD(P)/jDxRrv3z">NAD(P)</a>-dependent L-lactate dehydrogenase. Other LDHs act on D-lactate and/or are dependent on <a href="/facts/Cytochrome_c/8gXbxw9z">cytochrome c</a>: <a href="/facts/D-lactate_dehydrogenase_(cytochrome)/PxItSpbc">D-lactate dehydrogenase (cytochrome)</a> and <a href="/facts/L-lactate_dehydrogenase_(cytochrome)/EV20pCky">L-lactate dehydrogenase (cytochrome)</a>. 
LDH is expressed extensively in body tissues, such as blood cells and heart muscle. Because it is released during tissue damage, it is a marker of common injuries and disease such as heart failure.

Lactate dehydrogenase open-in-new

Lactate dehydrogenase