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Literature summary for 2.4.1.1 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
Search for more literature for 2.4.1.1

Activating Compound

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

Crystallization (Commentary)

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

General Stability

General Stability Organism
dithiothreitol stabilizes Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
DTNB
-
 Homo sapiens
DTNB
-
 Oryctolagus cuniculus

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

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

Source Tissue

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

Storage Stability

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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
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]

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