CATH Domain 5o50A01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.40	3-Layer(aba) Sandwich
	3.40.50	Rossmann fold
	3.40.50.2000	Glycogen Phosphorylase B;

Domain Context

CATH Clusters

Superfamily	Glycogen Phosphorylase B;
Functional Family	Glycogen phosphorylase, muscle form

Enzyme Information

2.4.1.1

Glycogen phosphorylase.

based on mapping to UniProt P00489

((1->4)-alpha-D-glucosyl)(n) + phosphate = ((1->4)-alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.

-!- This entry covers several enzymes from different sources that act in vivo on different forms of (1->4)-alpha-D-glucans. -!- Some of these enzymes catalyze the first step in the degradation of large branched glycan polymers - the phosphorolytic cleavage of alpha-1,4-glucosidic bonds from the non-reducing ends of linear poly(1->4)-alpha-D-glucosyl chains within the polymers. -!- The enzyme stops when it reaches the fourth residue away from an alpha-1,6 branching point, leaving a highly branched core known as a limit dextrin. -!- The description (accepted name) of the enzyme should be modified for each specific instance by substituting 'glycogen' with the name of the natural substrate, e.g. maltodextrin phosphorylase, starch phosphorylase, etc.

UniProtKB Entries (1)

P00489

PYGM_RABIT

Oryctolagus cuniculus

Glycogen phosphorylase, muscle form

PDB Structure

PDB	5O50
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Nanomolar Inhibitors of Glycogen Phosphorylase Based on beta-d-Glucosaminyl Heterocycles: A Combined Synthetic, Enzyme Kinetic, and Protein Crystallography Study. Bokor, E., Kyriakis, E., Solovou, T.G.A., Koppany, C., Kantsadi, A.L., Szabo, K.E., Szakacs, A., Stravodimos, G.A., Docsa, T., Skamnaki, V.T., Zographos, S.E., Gergely, P., Leonidas, D.D., Somsak, L. J. Med. Chem.