calm-2

Cystathionine Gamma-Lyase (CTH) belongs to the trans-sulfuration enzymes family. CTH exists as a homotetramer and interacts with CALM in a calcium-dependent manner. CTH breaks down cystathionine into cysteine, ammonia and 2-oxobutanoate. CTH catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine and has broad substrate specificity. Defects in CTH will lead to cystathioninuria, which is an autosomal recessive phenotype characterized by abnormal accumulation of plasma cystathionine.

Calmodulin (CaM) is a multifunctional intermediate calcium-binding messenger protein expressed in all eukaryotic cells. It is an intracellular target of the secondary messenger Ca2+, and the binding of Ca2+ is required for the activation of Calmodulin. Once bound to Ca2+, Calmodulin acts as part of a calcium signal transduction pathway by modifying its interactions with various target proteins such as kinases or phosphatases. Calmodulin is a small, highly conserved protein that is 148 amino acids long. The protein has two approximately symmetrical globular domains each containing a pair of EF-hand motifs (the N- and C-domain) separated by a flexible linker region for a total of four Ca2+ binding sites. Calmodulin mediates many crucial processes such as inflammation, metabolism, apoptosis, smooth muscle contraction, intracellular movement, short-term and long-term memory, and the immune response. Calmodulin is expressed in many cell types and can have different subcellular locations, including the cytoplasm, within organelles, or associated with the plasma or organelle membranes, but it is always found intracellularly.