Serine dehydratase or -serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structural and chemical properties vary greatly among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. The mechanism it catalyzes is the deamination of -serine to yield pyruvate, with the release of ammonia.
This enzyme has 1 substrate, -serine, and two products, pyruvate and NH3, and uses 1 cofactor, pyridoxal phosphate (PLP). The enzyme's main role is in gluconeogenesis in the liver's cytoplasm. By orienting the substrates and utilizing the PLP coenzyme, SDH lowers the activation energy to convert L-Serine into pyruvate, which can then be converted into glucose.
Read more about Serine Dehydratase: Nomenclature, Enzyme Structure, Enzyme Mechanism, Inhibitors, Biological Function, Disease Relevance, Evolution, External Links