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Literature summary for 2.4.2.4 extracted from

  • Panova, N.; Alexeev, C.; Polyakov, K.; Gavryushov, S.; Kritzyn, A.; Mikhailov, S.
    Substrate specificity of thymidine phosphorylase of E. coli: role of hydroxyl groups (2008), Nucleosides Nucleotides Nucleic Acids, 27, 1211-1214.
    View publication on PubMed
Search for more literature for 2.4.2.4

Inhibitors

Inhibitors Comment Organism Structure
additional information inhibitory nucleotide derivatives, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
thymidine + phosphate Escherichia coli
-
 thymine + 2-deoxy-alpha-D-ribose 1-phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the 3'-OH group is important for nucleotide binding, substrate analogues and substrate specificity, overview Escherichia coli ?
-
 ?
thymidine + phosphate
-
 Escherichia coli thymine + 2-deoxy-alpha-D-ribose 1-phosphate
-
 r
thymidine + phosphate substrate binding induces domain movement, which leads to the closed conformation of the active site and initiates phosphorylation, molecular dynamic simulation, overview Escherichia coli thymine + 2-deoxy-alpha-D-ribose 1-phosphate
-
 r

Subunits

Subunits Comment Organism
More three-dimensional enzyme structure by molecular dynamic simulation Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
 assay at Escherichia coli

General Information

General Information Comment Organism
metabolism the enzyme participates in the thymidine salvage pathway maintaining the thymidine pool in the cell Escherichia coli