Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | no metal binding | Oryctolagus cuniculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(1,4-alpha-D-glucosyl)n + phosphate | Oryctolagus cuniculus | polysaccharide substrate is glycogen, first step in glycogen breakdown removing one glucose at a time | (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Oryctolagus cuniculus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
muscle | - |
Oryctolagus cuniculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(1,4-alpha-D-glucosyl)n + phosphate | polysaccharide substrate is glycogen, first step in glycogen breakdown removing one glucose at a time | Oryctolagus cuniculus | (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate | - |
r | |
(1,4-alpha-D-glucosyl)n + phosphate | polysaccharide substrate is glycogen, phosphorolysis is the preferred reaction | Oryctolagus cuniculus | (1,4-alpha-D-glucosyl)n-1 + alpha-D-glucose 1-phosphate | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | enzyme has 2 distinct Rossmann domains separated by a large cleft that permits important flexibility, crystal structure, 1A8I, comparison with the glycogen synthase and amino acid sequence alignment | Oryctolagus cuniculus |
Synonyms | Comment | Organism |
---|---|---|
glycogen phosphorylase | - |
Oryctolagus cuniculus |
GP | - |
Oryctolagus cuniculus |
More | enzyme belongs to the GT-B-fold glycosyltransferase superfamily | Oryctolagus cuniculus |