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Literature summary extracted from

  • Boeck, B.; Schinzel, R.
    Purification and characterisation of an alpha-glucan phosphorylase from the thermophilic bacterium Thermus thermophilus (1996), Eur. J. Biochem., 239, 150-155 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.1 alpha-D-glucose-methylenephosphonate competitive inhibitor Thermus thermophilus
2.4.1.1 gluconolactone competitive inhibitor Thermus thermophilus
2.4.1.1 NaAsO2 competitive inhibitor with respect to phosphate Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.1 1.2
-
 alpha-D-glucose 1-phosphate synthesis reaction, cosubstrate: maltotetraose, pH 6.5, 70°C Thermus thermophilus
2.4.1.1 1.7
-
 maltoheptaose degradation direction, cosubstrate: phosphate, pH 6.5, 30°C Thermus thermophilus
2.4.1.1 1.9
-
 phosphate degradation direction, cosubstrate: maltoheptaose, pH 6.5, 30°C Thermus thermophilus
2.4.1.1 2.2
-
 phosphate degradation direction, cosubstrate: maltoheptaose, pH 6.5, 70°C Thermus thermophilus
2.4.1.1 2.8
-
 maltotetraose degradation direction, cosubstrate: phosphate, pH 6.5, 30°C Thermus thermophilus
2.4.1.1 3.6
-
 maltoheptaose degradation direction, cosubstrate: phosphate, pH 6.5, 70°C Thermus thermophilus
2.4.1.1 4.8
-
 maltotetraose degradation direction, cosubstrate: phosphate, pH 6.5, 70°C Thermus thermophilus
2.4.1.1 12.7
-
 maltotetraose synthesis reaction, cosubstrate: alpha-D-glucose 1-phosphate, pH 6.5, 70°C Thermus thermophilus
2.4.1.1 13.4
-
 maltotriose synthesis reaction, cosubstrate: alpha-D-glucose 1-phosphate, pH 6.5, 70°C Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Thermus thermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.1.1
-
 Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.1 glycogen + phosphate
-
 Thermus thermophilus alpha-D-glucose 1-phosphate + ?
-
 ?
2.4.1.1 maltoheptaose + phosphate
-
 Thermus thermophilus maltohexaose + alpha-D-glucose 1-phosphate
-
 ?
2.4.1.1 maltotetraose + phosphate
-
 Thermus thermophilus maltotriose + alpha-D-glucose 1-phosphate
-
 r
2.4.1.1 maltotriose + alpha-D-glucose 1-phosphate
-
 Thermus thermophilus maltotetraose + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.1.1 dimer 2 * 90000, While at 25°C the subunit composition of the thermophilic enzyme is an octameric form, the preferential form at the optimum temperature of 70°C seems to be a dimer Thermus thermophilus
2.4.1.1 octamer 8 * 90000, While at 25°C the subunit composition of the thermophilic enzyme is an octameric form, the preferential form at the optimum temperature of 70°C seems to be a dimer Thermus thermophilus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.1 70
-
 in the pH range 5.5-6.5 Thermus thermophilus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.4.1.1 50 90 50°C: about 50% of maximal activity, 90°C: about 40% of maximal activity Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
2.4.1.1 pyridoxal 5'-phosphate the enzyme contains 1 M pyridoxal 5'-phosphate per M of subunit Thermus thermophilus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.1.1 0.1
-
 alpha-D-glucose-methylenephosphonate 70°C, pH not specified in the publication Thermus thermophilus
2.4.1.1 3.3
-
 gluconolactone 70°C, pH not specified in the publication Thermus thermophilus
2.4.1.1 4.1
-
 NaAsO2 70°C, pH not specified in the publication Thermus thermophilus