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Literature summary for 2.7.4.3 extracted from

  • Dinbergs, I.D.; Lindmark, D.G.
    Tritrichomonas foetus: purification and characterization of hydrogenosomal ATP:AMP phosphotransferase (adenylate kinase) (1989), Exp. Parasitol., 69, 150-156.
    View publication on PubMed
Search for more literature for 2.7.4.3

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoic acid) DTT reverses Tritrichomonas suis
P1,P5-diadenosine 5'-pentaphosphate specific inhibitor Tritrichomonas suis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.076 0.083 AMP
-
 Tritrichomonas suis
0.1
-
 ADP
-
 Tritrichomonas suis
0.195 0.203 ATP
-
 Tritrichomonas suis

Localization

Localization Comment Organism GeneOntology No. Textmining
hydrogenosome
-
 Tritrichomonas suis 42566
-

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ requirement Tritrichomonas suis
Co2+ about 50% as effective as Mg2+ Tritrichomonas suis
Mg2+ requirement Tritrichomonas suis
Mn2+ requirement, about 50% as effective as Mg2+ Tritrichomonas suis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
-
 Tritrichomonas suis

Organism

Organism UniProt Comment Textmining
Tritrichomonas suis
-
 bovine parasite
-

Purification (Commentary)

Purification (Comment) Organism
-
 Tritrichomonas suis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + AMP
-
 Tritrichomonas suis ADP + ADP
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 9
-
 Tritrichomonas suis