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Literature summary for 2.4.2.2 extracted from

  • Alexeev, C.S.; Sivets, G.G.; Safonova, T.N.; Mikhailov, S.N.
    Substrate specificity of E. coli uridine phosphorylase. Further evidences of high-syn conformation of the substrate in uridine phosphorolysis (2017), Nucleosides Nucleotides Nucleic Acids, 36, 107-121 .
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information linear regression analysis of the Michaelis-Menten and Lineweaver-Burk plots Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
uridine + phosphate Escherichia coli
-
uracil + alpha-D-ribose 1-phosphate
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli P0C037 pyrimidine/purine nucleoside phosphorylase
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2'-C-methyluridine + phosphate
-
Escherichia coli uracil + 2-C-methyl-alpha-D-ribose 1-phosphate
-
r
2'-deoxyuridine + phosphate
-
Escherichia coli uracil + 2-deoxy-alpha-D-ribose 1-phosphate
-
r
3'-C-methyluridine + phosphate
-
Escherichia coli uracil + 3-C-methyl-alpha-D-ribose 1-phosphate
-
r
3'-fluoro-3'-deoxyuridine + phosphate
-
Escherichia coli uracil + 3'-fluoro-3'-deoxy-alpha-D-ribose 1-phosphate
-
r
4-thiouridine + phosphate
-
Escherichia coli 4-thiouracil + alpha-D-ribose 1-phosphate
-
r
5'-azido-5'-deoxythymidine + phosphate
-
Escherichia coli thymine + 5-azido-5-deoxy-alpha-D-ribose 1-phosphate
-
r
5'-bromo-5'-deoxythymidine + phosphate
-
Escherichia coli thymine + 5-bromo-5-deoxy-alpha-D-ribose 1-phosphate
-
r
5'-chloro-5'-deoxythymidine + phosphate
-
Escherichia coli thymine + 5'-chloro-5'-deoxy-alpha-D-ribose 1-phosphate
-
r
5'-deoxy-5'-methyleneuridine + phosphate
-
Escherichia coli uracil + 5-deoxy-5'-methylene-alpha-D-ribose 1-phosphate
-
r
5'-deoxythymidine + phosphate
-
Escherichia coli thymine + 5-deoxy-alpha-D-ribose 1-phosphate
-
r
5'-deoxyuridine + phosphate
-
Escherichia coli uracil + 5-deoxy-alpha-D-ribose 1-phosphate
-
r
5'-homothymidine + phosphate
-
Escherichia coli thymine + 5-homo-alpha-D-ribose 1-phosphate
-
r
5'-homouridine + phosphate
-
Escherichia coli uracil + 5-homo-alpha-D-ribose 1-phosphate
-
r
5'-iodo-5'-deoxythymidine + phosphate
-
Escherichia coli thymine + 5-iodo-5-deoxy-alpha-D-ribose 1-phosphate
-
r
5-C-methyluridine + phosphate
-
Escherichia coli 5-C-methyluracil + alpha-D-ribose 1-phosphate
-
r
5-methyluridine + phosphate
-
Escherichia coli 5-methyluracil + alpha-D-ribose 1-phosphate
-
r
6-methyluridine + phosphate
-
Escherichia coli 6-methyluracil + alpha-D-ribose 1-phosphate
-
r
additional information kinetic constants of the phosphorolysis reaction of uridine derivatives modified at 2'-, 3'- and 5'-positions of the sugar moiety and 2-, 4-, 5- and 6-positions of the heterocyclic base are determined. The absence of the 2'- or 5'-hydroxyl group is not crucial for successful binding and phosphorolysis. On the other hand, absence of both the 2'- and 5'-hydroxyl groups leads to loss of substrate binding to the enzyme. Substrate specificity, overview. 2,2'-O-Anhydrouridine, that models the high-syn conformation of uridine, binds better to the enzyme than uridine, despite the absence of a proton in the 3-position of the heterocyclic base, thus playing an important role in the substrate binding. In this case, the orientation of the heterocycle substantially outweighs the contribution of hydrogen bonding by the 2'-hydroxyl and 3-NH groups in the active site of enzyme UP. This strongly suggests that the 2-oxo group is located quite close to 2'-H in the substrate-UP complex. This is in line with the lack of substrate properties of 2-thiouridine Escherichia coli ?
-
-
uridine + phosphate
-
Escherichia coli uracil + alpha-D-ribose 1-phosphate
-
r

Subunits

Subunits Comment Organism
homodimer 2 * 27500 Escherichia coli

Synonyms

Synonyms Comment Organism
pyrimidine/purine nucleoside phosphorylase UniProt Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Escherichia coli