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Literature summary extracted from

  • Iltzsch, M.H.; El Kouni, M.H.; Cha, S.
    Kinetic studies of thymidine phosphorylase from mouse liver (1985), Biochemistry, 24, 6799-6807.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.4 2-deoxy-D-ribose product inhibition Mus musculus
2.4.2.4 thymine product inhibition; substrate inhibition Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.4 0.019
-
 phosphate
-
 Mus musculus
2.4.2.4 0.141
-
 thymine
-
 Mus musculus
2.4.2.4 0.945
-
 thymidine
-
 Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.4 Mus musculus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.4 thymidine + phosphate = thymine + 2-deoxy-alpha-D-ribose 1-phosphate rapid equilibrium random bi-bi mechanism with an enzyme-phosphate-thymine dead-end complex Mus musculus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.2.4 liver
-
 Mus musculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.4 additional information the enzyme in some tissues also catalyzes deoxyribonucleosyltransferase reaction of the type catalyzed by EC 2.4.2.6: 2-deoxy-D-ribosyl-base1 + base2 = 2-deoxy-D-ribosyl-base2 + base1 Mus musculus ?
-
 ?
2.4.2.4 thymidine + phosphate
-
 Mus musculus thymine + 2-deoxy-D-ribose 1-phosphate
-
 r