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Literature summary extracted from

  • Assaf, S.A.; Yunis, A.A.
    Physicochemical and catalytic properties of crystallized human muscle glycogen phosphorylase (1973), Ann. N. Y. Acad. Sci., 210, 139-152.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.1 dithiothreitol required to maintain activity Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.1 dialysis against 50 mM Tris and 40 mM 2-mercaptoethanol, pH 6.8 at 0°C Homo sapiens

General Stability

EC Number General Stability Organism
2.4.1.1 dithiothreitol stabilizes Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.1 DTNB
-
 Homo sapiens
2.4.1.1 DTNB
-
 Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.1 additional information
-
 additional information kinetic data Homo sapiens
2.4.1.1 additional information
-
 additional information kinetic data Oryctolagus cuniculus
2.4.1.1 additional information
-
 additional information kinetic data Homarus americanus
2.4.1.1 additional information
-
 additional information kinetic data Carcharhinus falciformis
2.4.1.1 additional information
-
 additional information comparison of muscle phosphorylases of various animals Homo sapiens
2.4.1.1 additional information
-
 additional information comparison of muscle phosphorylases of various animals Oryctolagus cuniculus
2.4.1.1 additional information
-
 additional information comparison of muscle phosphorylases of various animals Homarus americanus
2.4.1.1 additional information
-
 additional information comparison of muscle phosphorylases of various animals Carcharhinus falciformis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.1 175000
-
 phosphorylase b, sucrose density gradient centrifugation Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Carcharhinus falciformis
-
 silky shark
-
2.4.1.1 Homarus americanus
-
 American lobster
-
2.4.1.1 Homo sapiens
-
-
-
2.4.1.1 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.1 muscle
-
 Homo sapiens
-
2.4.1.1 muscle
-
 Oryctolagus cuniculus
-
2.4.1.1 muscle
-
 Homarus americanus
-
2.4.1.1 muscle
-
 Carcharhinus falciformis
-

Storage Stability

EC Number Storage Stability Organism
2.4.1.1 storage in frozen or lyophilized state, crystalline human, not rabbit, phosphorylase a or b, stable to Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate
-
 Homo sapiens [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate
-
 Oryctolagus cuniculus [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate
-
 Homarus americanus [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate
-
 Carcharhinus falciformis [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.4.1.1 More phosphorylase a dissociates into active dimers in the presence of high salt concentration, glucose or glycogen, human enzyme at 5 mg/ml protein concentration, the rabbit enzyme remains a tetramer even at 1 mg/ml Homo sapiens
2.4.1.1 More phosphorylase a dissociates into active dimers in the presence of high salt concentration, glucose or glycogen, human enzyme at 5 mg/ml protein concentration, the rabbit enzyme remains a tetramer even at 1 mg/ml Oryctolagus cuniculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.1 45
-
 crystalline, several h stable Homo sapiens