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Literature summary for 2.4.2.4 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
?
thymidine + phosphate
-
Mus musculus thymine + 2-deoxy-D-ribose 1-phosphate
-
r