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Literature summary for 2.4.2.1 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

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

Organism

Organism UniProt Comment Textmining
Cellulomonas sp.
-
-
-

Substrates and Products (Substrate)

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

Ki Value [mM]

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