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Overview for MACiE Entry M0209

Version history

General Information

EC Number: 2.7.1.20 (A member of the Transferases, Transferring phosphorus-containing groups, Phosphotransferases with an alcohol group as acceptor)

Enzyme Name: adenosine kinase

Biological Species: Toxoplasma gondii (Bacteria)

Catalytic Chain UniprotKB Accession Codes:

Representative PDB Code: 1lij - STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO PRODRUG 27-IODOTUBERCIDIN AND AMP-PCP (Resolution = 1.86 Å).

Catalytic CATH Codes:

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Overall Reaction:

Image of ATP

Image of Adenosine

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Image of ADP

Image of AMP

ATP
C00002
CHEBI:30616
Adenosine
C00212
CHEBI:16335
ADP
C00008
CHEBI:456216
AMP
C00020
CHEBI:456215

Overall Comment: Upon adenosine binding, a conserved dipeptide Gly68-Gly69 at the active site triggers a rigid-body rotation of 30 degrees of the lid domain, resulting in occlusion of the adenosine and the gamma-phosphate of ATP from the solvent. The reaction is ordered with adenosine binding first. This binding results in structural changes which are required in order for ATP to bind. The binding of ATP induces the formation of an anion hole, which completes the structural requirements for catalysis [1]. Although a chloride ion is bound in the active site, its role, if any, is unknown [1].


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Stepwise Description of the Reaction

Step 1Asp318 deprotonates the -CH2-OH group of the adeonsine substrate, which initiates a nucleophilic substitution against the gamma-phosphate of ATP. This produces the ADP and AMP products.
Step 2Water deprotonates Asp318 in an inferred return step.

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Catalytic Residues Involved

Type Number Chain Location of Function
Arg 136 A Side Chain
Asp 318 A Side Chain

Metal Cofactors for M0209

Type Het group Number Chain
magnesium MG 999 _ Overview

References

  1. M. A. Schumacher et al. (2000), J. Mol. Biol., 298, 875-893. Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.
    Medline: 10801355
  2. M. C. Maj et al. (2000), Biochem. Biophys. Res. Commun., 275, 386-393. Structure-activity studies on mammalian adenosine kinase.
    Medline: 10964675

Homologue information for M0209 (1lij)

CSA Homologues

MACiE Homologues (within the PDB)

MACiE Homologues (within UniprotKB/SwissProt)


Links to this entry in other databases

Link to EC-PDB-SUM Link to PDB-SUM Link to RCSB PDB Link to PDBe Link to CSA
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Link to EzCatDB

GOA logo
nucleotide binding (molecular function)
adenosine kinase activity (molecular function)
ATP binding (molecular function)
purine ribonucleoside salvage (biological process)
AMP biosynthetic process (biological process)
kinase activity (molecular function)
phosphorylation (biological process)
transferase activity (molecular function)
phosphotransferase activity, alcohol group as acceptor (molecular function)
metal ion binding (molecular function)
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