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Literature summary extracted from

  • Becker, J.U.; Wingender-Drissen, R.; Schiltz, E.
    Purification and properties of phosphorylase from bakers yeast (1983), Arch. Biochem. Biophys., 225, 667-678.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.1 phosphate activation Saccharomyces cerevisiae
2.4.1.1 phosphate phosphate content correlates with activity Saccharomyces cerevisiae
2.4.1.1 phosphate 0.1-0.74 mol covalently bound phosphate per mol subunit Saccharomyces cerevisiae
2.4.1.1 Phosphorylase kinase activation Saccharomyces cerevisiae
2.4.1.1 Phosphorylase kinase incorporates 1 mol phosphate per mol subunit Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.1 Phosphorylase phosphatase reactivation by phosphorylase kinase Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.1 additional information
-
 additional information
-
 Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.4.1.1 100000
-
 2 * 100000, SDS-PAGE Saccharomyces cerevisiae

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Saccharomyces cerevisiae
-
 bottom fermenting brewer's yeast
-
2.4.1.1 Saccharomyces pastorianus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.1.1 side-chain modification activation of enzyme by phosphorylase kinase, inactivation by phosphorylase phosphatase is due to phosphorylation of a single threonine residue in the N-terminus of the large subunit Saccharomyces cerevisiae
2.4.1.1 side-chain modification phosphate-content correlates with activity Saccharomyces cerevisiae
2.4.1.1 side-chain modification 0.1-0.74 mol covalently bound phosphate per mol subunit Saccharomyces cerevisiae
2.4.1.1 side-chain modification activation by phosphorylation Saccharomyces cerevisiae

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.1 Streptomycin, ammonium sulfate, DEAE-Sephadex, Sephadex G-200 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.1 47.5
-
-
 Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
2.4.1.1 4°C, 20-25 mg/ml in 100 mM succinate buffer, 0.02% NaN3, 2-3 months, little loss of activity Saccharomyces cerevisiae

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
-
 Saccharomyces pastorianus [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate
-
 Saccharomyces cerevisiae [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r

Subunits

EC Number Subunits Comment Organism
2.4.1.1 dimer 2 * 100000, SDS-PAGE Saccharomyces cerevisiae
2.4.1.1 dimer presumably s- and l-subunit of very slight differences in molecular weight, less active: tetramer of l-subunit, inactive: octamer and larger oligomers Saccharomyces cerevisiae
2.4.1.1 More
-
 Saccharomyces pastorianus
2.4.1.1 More inactive enzyme tends to form larger oligomers Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.4.1.1 pyridoxal 5'-phosphate requirement Saccharomyces pastorianus
2.4.1.1 pyridoxal 5'-phosphate requirement Saccharomyces cerevisiae