Sandbox Reserved 346: Difference between revisions
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The large domain is where the active site of AST is found and to accomadate this the core is contains many alpha/beta supersecondary structures. This is contrasted with the core of the small subunit which is fromed from two alpha hellices and two beta strands. In multicellular organisms there is a kink at the 325th residue which acts as a hinge for the samll domain, which allows for the resulting conformational changes that take place upon the binding of inhibitors to the enzyme. | The large domain is where the active site of AST is found and to accomadate this the core is contains many alpha/beta supersecondary structures. This is contrasted with the core of the small subunit which is fromed from two alpha hellices and two beta strands. In multicellular organisms there is a kink at the 325th residue which acts as a hinge for the samll domain, which allows for the resulting conformational changes that take place upon the binding of inhibitors to the enzyme. | ||
As was stated above, the active site of AST is situated on the large domain of the subunit. Within the active site is the amino residue Lys 258, also known as the intternal aldimine, which binds with the cofactor Pyridoxal 5'-phosphate (<scene name='Sandbox_Reserved_346/Plp/ | As was stated above, the active site of AST is situated on the large domain of the subunit. Within the active site is the amino residue Lys 258, also known as the intternal aldimine, which binds with the cofactor Pyridoxal 5'-phosphate (<scene name='Sandbox_Reserved_346/Plp/5'>PLP</scene>) forming what is called a Schiff base. Upon addition of an amino acid substrate a new Schiiff base forms between PLP and the amino acid | ||
=='''Function'''== | =='''Function'''== | ||