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Literature summary extracted from

  • Munagala, N.; Wang, C.C.
    The purine nucleoside phosphorylase from Trichomonas vaginalis is a homologue of the bacterial enzyme (2002), Biochemistry, 41, 10382-10389.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.4.2.1 medicine the enzyme constitutes a target for antitrichomonial chemotherapy Trichomonas vaginalis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.1 expression in Escherichia coli Trichomonas vaginalis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.2.1 Formycin A
-
 Trichomonas vaginalis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.2.1 6.1
-
 adenosine
-
 Trichomonas vaginalis
2.4.2.1 12.3
-
 adenine
-
 Trichomonas vaginalis
2.4.2.1 31.5
-
 Inosine
-
 Trichomonas vaginalis
2.4.2.1 35.9
-
 guanine
-
 Trichomonas vaginalis
2.4.2.1 45.6
-
 hypoxanthine
-
 Trichomonas vaginalis
2.4.2.1 59.7
-
 guanosine
-
 Trichomonas vaginalis

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.1 Trichomonas vaginalis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.2.1 recombinant enzyme Trichomonas vaginalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.1 adenosine + phosphate in the reverse reaction the catalytic activity with adenine is higher than that with either hypoxanthine or guanine Trichomonas vaginalis adenine + alpha-D-ribose 1-phosphate
-
 r
2.4.2.1 guanosine + phosphate
-
 Trichomonas vaginalis guanine + alpha-D-ribose 1-phosphate
-
 r
2.4.2.1 inosine + phosphate
-
 Trichomonas vaginalis hypoxanthine + alpha-D-ribose 1-phosphate
-
 r