Cystathionine gamma-lyase (CSE) is a member of the gamma family of PLP-dependent enzymes (which bind to pyridoxal-5'-phosphate for reaction catalysis), along with other enzymes such as cystathionine gamma-synthase, Cystathionine beta-lyase, and Methionine gamma-lyase. Similar to other enzymes in this family, CSE exhibits a tetrameric structure with D2 symmetry.
Functions
Structure
Cystathionine gamma-lyase exhibits a tetrameric quaternary structure when bound to its ligand (PLP), and in its apo form, it can exist as both a monomer and a tetramer, with the latter being more predominant [1]. The monomer comprises two domains: a .
The is characterized by the presence of an alpha/beta/alpha structure, and a mixed beta-sheet surrounded by eight alpha-helices. On the other hand, the possesses a four-stranded antiparallel beta-sheet and three alpha-helices on one side of the beta-sheet.
Disease
Structural highlights
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