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Literature summary for 2.4.1.1 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
Search for more literature for 2.4.1.1

Activating Compound

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

Inhibitors

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

KM Value [mM]

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

Molecular Weight [Da]

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

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
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
side-chain modification phosphate-content correlates with activity Saccharomyces cerevisiae
side-chain modification 0.1-0.74 mol covalently bound phosphate per mol subunit Saccharomyces cerevisiae
side-chain modification activation by phosphorylation Saccharomyces cerevisiae

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability Organism
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[(1->4)-alpha-D-glucosyl]n + phosphate
-
 Saccharomyces pastorianus [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r
[(1->4)-alpha-D-glucosyl]n + phosphate
-
 Saccharomyces cerevisiae [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
 r

Subunits

Subunits Comment Organism
dimer 2 * 100000, SDS-PAGE Saccharomyces cerevisiae
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
More
-
 Saccharomyces pastorianus
More inactive enzyme tends to form larger oligomers Saccharomyces cerevisiae

Cofactor

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