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Literature summary extracted from

  • Wielgus-Kutrowska, B.; Bzowska, A.
    Kinetic properties of Cellulomonas sp. purine nucleoside phosphorylase with typical and non-typical substrates: implications for the reaction mechanism (2005), Nucleosides Nucleotides Nucleic Acids, 24, 471-476.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.1 alpha-D-ribose 1-phosphate mixed inhibition Cellulomonas sp.
2.4.2.1 guanine competitive versus phosphate and inosine Cellulomonas sp.
2.4.2.1 guanosine uncompetitive inhibition of alpha-D-ribose 1-phosphate Cellulomonas sp.
2.4.2.1 phosphate uncompetitive versus guanine Cellulomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.1 Cellulomonas sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.1 7-methylguanosine + phosphate
-
 Cellulomonas sp. 7-methylguanine + alpha-D-ribose 1-phosphate
-
 r
2.4.2.1 guanine + alpha-D-ribose 1-phosphate
-
 Cellulomonas sp. guanosine + phosphate
-
 ?
2.4.2.1 inosine + phosphate
-
 Cellulomonas sp. hypoxanthine + alpha-D-ribose 1-phosphate
-
 r

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.2.1 0.0025
-
 guanine versus phosphate Cellulomonas sp.
2.4.2.1 0.0036
-
 guanine versus inosine Cellulomonas sp.
2.4.2.1 0.8
-
 guanosine versus alpha-D-ribose 1-phosphate Cellulomonas sp.
2.4.2.1 4.7
-
 phosphate versus guanine Cellulomonas sp.