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Human Cystathionine gamma lyase |
Cystathionine-γ-lyase (EC 4.4.1.1, CTH, cystathionase) is a pyridoxal-phosphate (PLP) dependent enzyme that catalyses the conversion of L-cystathionine to L-cysteine in the transulfuration pathway. Deficiency of CTH causes the autosomal recessive disease cystathioninemia. CTH can also convert L-cysteine to H2S. This gas transmitter is highly interesting from a medical perspective since it functions as a neuromodulator in the central nervous system and as a smooth muscle relaxant in the vascular system. It has also been suggested to be linked to several cardiovascular diseases, to (anti-) inflammatory responses and to gastric injury caused by non-steroidal anti-inflammatory drugs. H2S is produced in the liver, kidney, vascular system and gut by CTH and in the brain by cystathionine beta-synthetase (CBS). Overexpression of CTH inhibits cell proliferation, induces cell death and is linked to inflammation. Here we present the crystal-structure of CTH at 2.6Å resolution. The enzyme is crystallized as a tetramer with PLP observed covalently bound to Lys212 forming a Schiff base in three out of four active sites. Both monomers in the subunit interfaces contribute to the active site pocket.
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