Phosphorylase Kinase
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Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Phosphorylase kinase is a serine/threonine-specific protein kinase which converts glycogen phosphorylase b to glycogen phosphorylase a, activating it to release glucose-1-phosphate from glycogen. The protein is a homotetramer of tetramers, which each of the four tetramers possessing an , , , and subunit. The (gamma) subunit is the site of the enzyme''s catalytic activity, i.e. the conversion of glycogen phosphorylase b to glycogen phosphorylase a. The other three…mehr

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Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Phosphorylase kinase is a serine/threonine-specific protein kinase which converts glycogen phosphorylase b to glycogen phosphorylase a, activating it to release glucose-1-phosphate from glycogen. The protein is a homotetramer of tetramers, which each of the four tetramers possessing an , , , and subunit. The (gamma) subunit is the site of the enzyme''s catalytic activity, i.e. the conversion of glycogen phosphorylase b to glycogen phosphorylase a. The other three subunits regulate the enzyme''s activity and, when unmodified by the binding of calcium or phosphorylation, are inhibitory.