4kh5: Difference between revisions
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==About this Structure== | ==About this Structure== | ||
[[4kh5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | [[4kh5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgo Toxgo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KH5 OCA]. | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:024115522</ref><references group="xtra"/><references/> | <ref group="xtra">PMID:024115522</ref><references group="xtra"/><references/> | ||
[[Category: Nucleoside-triphosphatase]] | [[Category: Nucleoside-triphosphatase]] | ||
[[Category: | [[Category: Toxgo]] | ||
[[Category: Krug, U.]] | [[Category: Krug, U.]] | ||
[[Category: Strater, N.]] | [[Category: Strater, N.]] | ||
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[[Category: Actin-like fold]] | [[Category: Actin-like fold]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Ntpdase]] | |||
Revision as of 11:51, 25 December 2013
Toxoplasma gondii NTPDase1 C258S/C268S in complex with Mg and AMPNPToxoplasma gondii NTPDase1 C258S/C268S in complex with Mg and AMPNP
Template:ABSTRACT PUBMED 24115522
FunctionFunction
[NTP2_TOXGO] May perform an important processing step in the conversion of high energy nucleotides prior to uptake by the parasite. NTPAse-II has a specific activity 4.5-fold lower than NTPAse-I in hydrolysis of ATP. The primary difference between these isozymes lies in their ability to hydrolyze nucleoside triphosphate versus diphosphate substrates. While NTPAse-II hydrolyzes ATP to ADP and ADP to AMP at almost the same rate, NTPAse-I hydrolyzes ADP to AMP at a much slower rate (0.7% of the rate for ATP).
About this StructureAbout this Structure
4kh5 is a 2 chain structure with sequence from Toxgo. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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