Ectonucleoside triphosphate diphosphohydrolase

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== Function ==
== Function ==
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'''Ectonucleoside triphosphate diphosphohydrolase (NTPDase)''' hydrolyzes nucleoside 5’-triphosphate to nucleoside 5’-phosphate and 2 phosphates. NTPDase can hydrolyze ATP and ADP. NTPDase has an important role in regulating neutrophil chemotaxis. NTPDase 1,2,3,8 are cell surface enzymes with catalytic sites facing extracellularly while other NTPDases act intracellularly. NTPDase require Ca<sup>+2</sup> or Mg<sup>+2</sup> for their activity. The NTPDases can be differentiated according to their substrate specificity, divalent cation usage and product formation.
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'''Ectonucleoside triphosphate diphosphohydrolase (NTPDase)''' hydrolyzes nucleoside 5’-triphosphate to nucleoside 5’-phosphate and 2 phosphates. NTPDase can hydrolyze ATP and ADP. NTPDase has an important role in regulating neutrophil chemotaxis. NTPDase 1,2,3,8 are cell surface enzymes with catalytic sites facing extracellularly while other NTPDases act intracellularly. NTPDase require Ca<sup>+2</sup> or Mg<sup>+2</sup> for their activity. The NTPDases can be differentiated according to their substrate specificity, divalent cation usage and product formation.<ref>PMID:23830739</ref>
== Disease ==
== Disease ==

Revision as of 10:52, 11 January 2016

Structure of NTDPase1 complex with GMPPNP, Na+ (purple), Cl- (large green), Mg+2 (small green) ions (PDB code 4brg).

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3D structures of ectonucleoside triphosphate diphosphohydrolase

Updated on 11-January-2016

References

  1. Zebisch M, Krauss M, Schafer P, Lauble P, Strater N. Crystallographic Snapshots along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases. Structure. 2013 Jul 2. pii: S0969-2126(13)00200-1. doi:, 10.1016/j.str.2013.05.016. PMID:23830739 doi:10.1016/j.str.2013.05.016

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