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Literature summary for 2.7.1.20 extracted from

  • Naguib, F.N.; Rais, R.H.; Al Safarjalani, O.N.; el Kouni, M.H.
    Kinetic mechanism of Toxoplasma gondii adenosine kinase and the highly efficient utilization of adenosine (2015), Comp. Biochem. Physiol. B, 188, 63-69.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.20

Inhibitors

Inhibitors Comment Organism Structure
adenosine substrate inhibition, presence of ATP relieves substrate inhibition by adenosine Toxoplasma gondii
ADP noncompetitive with adenosine, ADP and ATP show additive effects Toxoplasma gondii
AMP competitive with ATP, noncompetitive with adenosine Toxoplasma gondii
ATP noncompetitive with adenosine, ADP and ATP show additive effects Toxoplasma gondii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 adenosine pH 7.4, 37°C Toxoplasma gondii
0.05
-
 ATP pH 7.4, 37°C Toxoplasma gondii

Organism

Organism UniProt Comment Textmining
Toxoplasma gondii Q9TVW2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + adenosine 47.7% conversion Toxoplasma gondii 2 AMP
-
 ?
ATP + adenosine 96.2% conversion Toxoplasma gondii ADP + AMP
-
 ?
dADP + adenosine 28.5% conversion Toxoplasma gondii dAMP + AMP
-
 ?
GDP + adenosine 21.1% conversion Toxoplasma gondii GMP + AMP
-
 ?
additional information hybrid random bi-uni ping-pong uni-bi mechanism, with substrate-enzyme-cosubstrate complex formation, binding pattern indicates that binding of the substrate interferes with the binding of the cosubstrate and vice versa. For every ATP consumed, the enzyme generates three AMPs Toxoplasma gondii ?
-
 ?
UDP + adenosine 5.9% conversion Toxoplasma gondii UMP + AMP
-
 ?