Glycogen phosphorylase with a mass of 97.434 kDa in muscle cells. While the enzyme can exist as an inactive monomer or tetramer, it is biologically active as a dimer of two identical subunits. In mammals, the major isozymes of glycogen phosphorylase are found in muscle, liver, and brain. The brain type is predominant in adult brain and embryonic tissues, whereas the liver and muscle types are predominant in adult liver and skeletal muscle, respectively. The glycogen phosphorylase dimer has many regions of biological significance, including catalytic sites, glycogen binding sites, allosteric sites, and a reversibly phosphorylated serine residue. First, the catalytic sites
(glycogen-synthase-D) phosphatase 2_degree_C. (glycogen-synthase-D) phosphatase In enzymology, a [glycogen-synthase-D] phosphatase () is an enzyme that catalyzes the chemical reaction Thus, the two substrates of this enzyme are glycogen-synthase D and HO, whereas its two products are glycogen-synthase I and phosphate. This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is [UDP-glucose:glycogen 4-alpha-D-glucosyltransferase-D] phosphohydrolase. Other names in common use include uridine diphosphoglucose-glycogen glucosyltransferase phosphatase, UDP-glycogen glucosyltransferase phosphatase, UDPglucose-glycogen glucosyltransferase phosphatase, glycogen glucosyltransferase phosphatase, glycogen synthetase phosphatase, glycogen synthase phosphatase, glycogen synthase D phosphatase, Mg dependent glycogen synthase phosphatase, and phosphatase