CATH Classification

Domain Context

CATH Clusters

Superfamily Glycogen Phosphorylase B;
Functional Family Alpha-1,4 glucan phosphorylase

Enzyme Information

2.4.1.1
Glycogen phosphorylase.
based on mapping to UniProt P06738
((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)

P06738
PHSG_YEAST
Saccharomyces cerevisiae S288C
Glycogen phosphorylase

PDB Structure

PDB 1YGP
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
A protein phosphorylation switch at the conserved allosteric site in GP.
Lin, K., Rath, V.L., Dai, S.C., Fletterick, R.J., Hwang, P.K.
Science