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Literature summary for 2.4.2.1 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
Search for more literature for 2.4.2.1

Application

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

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Trichomonas vaginalis

Inhibitors

Inhibitors Comment Organism Structure
Formycin A
-
 Trichomonas vaginalis

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Trichomonas vaginalis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Trichomonas vaginalis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
guanosine + phosphate
-
 Trichomonas vaginalis guanine + alpha-D-ribose 1-phosphate
-
 r
inosine + phosphate
-
 Trichomonas vaginalis hypoxanthine + alpha-D-ribose 1-phosphate
-
 r