Difference between revisions of "Phosphatase Family PHP"
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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_PHP|PHP Superfamily]]: [[Phosphatase_Famiyl_PHP|PHP Family]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_PHP|PHP Superfamily]]: [[Phosphatase_Famiyl_PHP|PHP Family]] | ||
| − | This superfamily has a single family, subfamily and gene PHPT1 in human. It is found throughout eukaryotes, though lost from fungi. In most species, it is a single-copy gene, but four were found in fruit fly. | + | This superfamily has a single family, subfamily and gene PHPT1 in human. It is found throughout eukaryotes, though lost from fungi. In most species, it is a single-copy gene, but four were found in fruit fly. It's catalytic domain has been solved and a potential enzymatic mechanism proposed <cite>Gong</cite>. Its fold is not related to that of any other enzyme. |
| Line 15: | Line 15: | ||
== References == | == References == | ||
<biblio> | <biblio> | ||
| + | #Gong pmid=18991813 | ||
#Maurer04 pmid=16039992 | #Maurer04 pmid=16039992 | ||
#Klumpp03 pmid=12788074 | #Klumpp03 pmid=12788074 | ||
Revision as of 01:11, 1 May 2014
Phosphatase Classification: PHP Superfamily: PHP Family
This superfamily has a single family, subfamily and gene PHPT1 in human. It is found throughout eukaryotes, though lost from fungi. In most species, it is a single-copy gene, but four were found in fruit fly. It's catalytic domain has been solved and a potential enzymatic mechanism proposed [1]. Its fold is not related to that of any other enzyme.
The known substrates are beta subunit of heterotrimeric G proteins [2], the metabolic enzyme adenosine 5’-triphosphate-citrate lyase (ACL) [3], and the Ca2+-activated K+ channel KCa3.1 [4]. These are known or suspected substrates of the nucleoside diphosphate kinases (NDK).
Involved in nervous system
Its role in neuronal cells is particularly interesting. In C. elegans, the ortholog is expressed exclusively in neurons [5]. In human cells, the overexpression of PHPT1 decreases the activity of ACL and reduces the viability of neuronal cells [6].
References
- Gong W, Li Y, Cui G, Hu J, Fang H, Jin C, and Xia B. Solution structure and catalytic mechanism of human protein histidine phosphatase 1. Biochem J. 2009 Mar 1;418(2):337-44. DOI:10.1042/BJ20081571 |
- Mäurer A, Wieland T, Meissl F, Niroomand F, Mehringer R, Krieglstein J, and Klumpp S. The beta-subunit of G proteins is a substrate of protein histidine phosphatase. Biochem Biophys Res Commun. 2005 Sep 9;334(4):1115-20. DOI:10.1016/j.bbrc.2005.06.200 |
- Klumpp S, Bechmann G, Mäurer A, Selke D, and Krieglstein J. ATP-citrate lyase as a substrate of protein histidine phosphatase in vertebrates. Biochem Biophys Res Commun. 2003 Jun 20;306(1):110-5. DOI:10.1016/s0006-291x(03)00920-3 |
- Srivastava S, Zhdanova O, Di L, Li Z, Albaqumi M, Wulff H, and Skolnik EY. Protein histidine phosphatase 1 negatively regulates CD4 T cells by inhibiting the K+ channel KCa3.1. Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14442-6. DOI:10.1073/pnas.0803678105 |
- Klumpp S, Hermesmeier J, Selke D, Baumeister R, Kellner R, and Krieglstein J. Protein histidine phosphatase: a novel enzyme with potency for neuronal signaling. J Cereb Blood Flow Metab. 2002 Dec;22(12):1420-4. DOI:10.1097/01.wcb.0000045041.03034.99 |
- Klumpp S, Faber D, Fischer D, Litterscheid S, and Krieglstein J. Role of protein histidine phosphatase for viability of neuronal cells. Brain Res. 2009 Apr 6;1264:7-12. DOI:10.1016/j.brainres.2008.12.052 |
