![]() ![]() Thus, the H1 structure indicated the final catalysis step prior to product release. The Asp79 residue was involved in coordination with the water molecule and functioned as an acid, facilitating the intermediate compound formation and hydrolyzation. At the catalytic pocket’s base, the Cys110 residue attacked phosphorous atoms during dephosphorylation, leading to a temporary enzyme-phosphate intermediate formation which underwent hydrolysis for inorganic phosphate and enzyme regeneration.Ĭys110 residue’s sulphur atom was positioned parallel to the P-O bond, corresponding to the bond formed when the enzyme was regenerated. ![]() The α1 helices from a single H1 protomer formed a bundled structure with three α4 to α6 helices of the corresponding promoters involved in pairing. ![]() The α1 N-terminal helices from every protomer interchanged for mediating H1 dimerizations. The Arg116 residue guaranteed efficient substrate orientation and binding.
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