Nucleoside triphosphatase
From Proteopedia
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'''Nucleoside triphosphatase''' or '''nucleoside triphosphate diphosphohydrolase''' (NTPase) is responsible for degradation of nucleotides to their monophosphate form. NTPase is found in mammals and in pathogenic microbes. In mammals NTPase hs a crucial role in regulation of purinergic signalling by hydrolysis of extracellular nucleotides. The function of NTPase in pathogens is still unknown<ref>PMID:24115522</ref>. | '''Nucleoside triphosphatase''' or '''nucleoside triphosphate diphosphohydrolase''' (NTPase) is responsible for degradation of nucleotides to their monophosphate form. NTPase is found in mammals and in pathogenic microbes. In mammals NTPase hs a crucial role in regulation of purinergic signalling by hydrolysis of extracellular nucleotides. The function of NTPase in pathogens is still unknown<ref>PMID:24115522</ref>. | ||
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| - | == Disease == | ||
== Relevance == | == Relevance == | ||
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| + | The modulation of NTPase activity sems a good therapeutic method for regulating the concentration of ATP. High ATP concentration has been shown to be involved in various disorders in the CNS including brain injury, ischemia, neuro-inflammation, epilepsy, neuropathic pain and migraine<ref>PMID:25694082</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
Revision as of 08:32, 12 May 2020
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3D structures of nucleoside triphosphatase
Updated on 12-May-2020
References
- ↑ Krug U, Totzauer R, Zebisch M, Strater N. The ATP/ADP Substrate Specificity Switch between Toxoplasma gondii NTPDase1 and NTPDase3 is Caused by an Altered Mode of Binding of the Substrate Base. Chembiochem. 2013 Oct 2. doi: 10.1002/cbic.201300441. PMID:24115522 doi:http://dx.doi.org/10.1002/cbic.201300441
- ↑ Roszek K, Czarnecka J. Is Ecto-nucleoside Triphosphate Diphosphohydrolase (NTPDase)-based Therapy of Central Nervous System Disorders Possible? Mini Rev Med Chem. 2015;15(1):5-20. doi: 10.2174/1389557515666150219114416. PMID:25694082 doi:http://dx.doi.org/10.2174/1389557515666150219114416
- ↑ Krug U, Zebisch M, Krauss M, Strater N. Structural insight into the activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reduction. J Biol Chem. 2011 Nov 30. PMID:22130673 doi:10.1074/jbc.M111.294348
