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CATH Superfamily 1.50.10.10

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was: waiting to be named.

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 18652: Phosphorylase kinase alpha/beta subunit

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Phosphorylase kinase. [EC: 2.7.11.19]
2 ATP + phosphorylase b = 2 ADP + phosphorylase a.
  • Requires calmodulin for activity.
  • The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b.
  • For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase.
  • The enzyme couples muscle contraction with energy production via glycogenolysis--glycolysis by catalyzing the Ca(2+)-dependent phosphorylation and activation of glycogen phosphorylase b.
  • The gamma subunit of the tetrameric alpha-beta-gamma-delta enzyme is the catalytic subunit.
  • Formerly EC 2.7.1.38.
 11 A0A061HV34 A0A061HX63 A0A061HYP0 A0A061I9B7 B7Z134 G3H5K2 M9NDS5 M9NGW5 M9PCI5 Q6IDE0
(1 more...)
Glycogen phosphorylase. [EC: 2.4.1.1]
((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.
 1 G4LWK2