FunctionAdenosine kinase (AdK) catalyzes the transfer of phosphate from ATP to adenosine to produce AMP. AMP-PCP is a non-hydrolyzable ATP analog.[1]
DiseaseAdK deficiency causes hypermethioninemia. Overexpression of AdK in the brain leads to decrease of adenosine and is believed as the main cause of epilepsy.
Structural highlightsAdK consists of a (PDB entry 1bx4).[2]
- . Water molecules are shown as red spheres.
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3D structures of adenosine kinaseAdenosine kinase 3D structures
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3D structures of adenosine kinase3D structures of adenosine kinase
Updated on 28-February-2019
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- Adenosine kinase
- 1lio – TgAdK – Toxoplasma gondii
- 2pkf – MtAdK – Mycobacterium tuberculosis
- 4n08 – TbAdK – Trypanosoma brucei
- Adenosine kinase binary complex
- 1bx4 – hAdK + adenosine - human
- 2i6a, 2i6b – hAdK + prodrug
- 4o1l – hAdK + inhibitor
- 1dgm, 1lik – TgAdK + adenosine
- 2a9y – TgAdK (mutant) + dimethyladenosine
- 2abs – TgAdK (mutant) + AMP-PCP
- 2aa0 – TgAdK (mutant) + methylthiopurine
- 2pkk, 4ube – MtAdK + fluoroadenosine
- 2pkn – MtAdK + AMP-PCP
- 2pkm – MtAdK + adenosine
- 4o1g – MtAdK + γ-thio-ATP
- 4pvv – MtAdK + inhibitor
- 5kb6 – mAdK + adenosine - mouse
- 3loo – AdK + adenosine tetraphosphate – Anopheles gambiae
- 2xtb – TbAdK + morpholine
- Adenosine kinase ternary complex
- 1lii – TgAdK + adenosine + AMP-PCP
- 2a9z – TgAdK (mutant) + dimethyladenosine + AMP-PCP
- 1lij – TgAdK + prodrug + AMP-PCP
- 2ab8 – TgAdK (mutant) + methylthiopurine + AMP-PCP
- 3ubo – AdK + adenosine + ADP – Sinorhizobium meliloti
- 4dc3 – AdK + adenosine + fluoroadenosine – Schistosoma masoni
- 4n09 – TbAdK + adenosine + ADP
- 5kb5 – mAdK + adenosine + ADP
ReferencesReferences
- ↑ Park J, Gupta RS. Adenosine kinase and ribokinase--the RK family of proteins. Cell Mol Life Sci. 2008 Sep;65(18):2875-96. doi: 10.1007/s00018-008-8123-1. PMID:18560757 doi:http://dx.doi.org/10.1007/s00018-008-8123-1
- ↑ Mathews II, Erion MD, Ealick SE. Structure of human adenosine kinase at 1.5 A resolution. Biochemistry. 1998 Nov 10;37(45):15607-20. PMID:9843365 doi:10.1021/bi9815445
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