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Glycosyl hydrolase family 65, N-terminal domain
This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyses the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity [1] although its precise function remains unknown. [1]. 11587643. Crystal structure of maltose phosphorylase from Lactobacillus. brevis: unexpected evolutionary relationship with glucoamylases.. Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H;. Structure (Camb) 2001;9:689-697. (from Pfam)
glycosyl hydrolase family 65 protein
This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyses the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown [1]. [1]. 11587643. Crystal structure of maltose phosphorylase from Lactobacillus. brevis: unexpected evolutionary relationship with glucoamylases.. Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H;. Structure (Camb) 2001;9:689-697. (from Pfam)
Glycosyl hydrolase family 65 central catalytic domain
This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyses the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom [1]. The catalytic domain also forms the majority of the dimerisation interface. [1]. 11587643. Crystal structure of maltose phosphorylase from Lactobacillus. brevis: unexpected evolutionary relationship with glucoamylases.. Egloff MP, Uppenberg J, Haalck L, van Tilbeurgh H;. Structure (Camb) 2001;9:689-697. (from Pfam)
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