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Glycogen phosphorylase domain structure

Figure 21.6 Structure of glycogen phosphorylase. This enzyme forms a homodimer one subunit is shown in white and the other in yellow. Each catalytic site includes a pyridoxal phosphate PLP group, linked to lysine 680 of the enzyme. The binding site for the phosphate (Pj) substrate is shown. Not icp that the catalytic site lies between the C-termina domain and the glycogen-binding site, A narrow crevice, which binds four or five glucose units of glycogen, connects the two sites. The separation of the sites allows the catalytic site to phosphorolyze several glucose units before the enzyme must rebind the glycogen substrate. [Drawn from INOl.pdb.]... Figure 21.6 Structure of glycogen phosphorylase. This enzyme forms a homodimer one subunit is shown in white and the other in yellow. Each catalytic site includes a pyridoxal phosphate PLP group, linked to lysine 680 of the enzyme. The binding site for the phosphate (Pj) substrate is shown. Not icp that the catalytic site lies between the C-termina domain and the glycogen-binding site, A narrow crevice, which binds four or five glucose units of glycogen, connects the two sites. The separation of the sites allows the catalytic site to phosphorolyze several glucose units before the enzyme must rebind the glycogen substrate. [Drawn from INOl.pdb.]...

See other pages where Glycogen phosphorylase domain structure is mentioned: [Pg.230]    [Pg.481]    [Pg.481]    [Pg.278]    [Pg.279]    [Pg.230]    [Pg.381]    [Pg.83]    [Pg.122]   
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Domain structure

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