AP3A hydrolase

Definition:

Hydrolyzes extracellular Ap3A into AMP and ADP, and Ap4A into AMP and ATP. Ap3A and Ap4A are diadenosine polyphosphates thought to induce proliferation of vascular smooth muscle cells. Acts as a procoagulant, mediating platelet aggregation at the site of nascent thrombus via release of ADP from Ap3A and activation of ADP receptors.

References:

[1]. Ronald A Albright, et al. NPP4 is a procoagulant enzyme on the surface of vascular endothelium. Blood. 2012 Nov 22;120(22):4432-40. [Content Brief]

[2]. C D Lima, et al. Structure-based analysis of catalysis and substrate definition in the HIT protein family. Science. 1997 Oct 10;278(5336):286-90. [Content Brief]

[3]. Andrzej Guranowski, et al. Fhit proteins can also recognize substrates other than dinucleoside polyphosphates. FEBS Lett. 2008 Sep 3;582(20):3152-8. [Content Brief]

[4]. S Semba, et al. Fhit modulation of the Akt-survivin pathway in lung cancer cells: Fhit-tyrosine 114 (Y114) is essential. Oncogene. 2006 May 11;25(20):2860-72. [Content Brief]

[5]. L D Barnes, et al. Fhit, a putative tumor suppressor in humans, is a dinucleoside 5',5"'-P1,P3-triphosphate hydrolase. Biochemistry. 1996 Sep 10;35(36):11529-35. [Content Brief]

[6]. Jörg Weiske, et al. The tumor suppressor Fhit acts as a repressor of beta-catenin transcriptional activity. Proc Natl Acad Sci U S A. 2007 Dec 18;104(51):20344-9. [Content Brief]

[7]. C Brenner, et al. Purification and crystallization of complexes modeling the active state of the fragile histidine triad protein. Protein Eng. 1997 Dec;10(12):1461-3. [Content Brief]

[8]. Alessandro Rimessi, et al. Intramitochondrial calcium regulation by the FHIT gene product sensitizes to apoptosis. Proc Natl Acad Sci U S A. 2009 Aug 4;106(31):12753-8. [Content Brief]

[9]. Anna M Wojdyła-Mamoń, et al. Adenylylsulfate-ammonia adenylyltransferase activity is another inherent property of Fhit proteins. Biosci Rep. 2015 Jun 25;35(4):e00235. [Content Brief]

[10]. Francesco Trapasso, et al. Designed FHIT alleles establish that Fhit-induced apoptosis in cancer cells is limited by substrate binding. Proc Natl Acad Sci U S A. 2003 Feb 18;100(4):1592-7. [Content Brief]

[11]. H C Pace, et al. Genetic, biochemical, and crystallographic characterization of Fhit-substrate complexes as the active signaling form of Fhit. Proc Natl Acad Sci U S A. 1998 May 12;95(10):5484-9. [Content Brief]

[12]. Kaisheng Huang, et al. The mechanism of action of the fragile histidine triad, Fhit: isolation of a covalent adenylyl enzyme and chemical rescue of H96G-Fhit. Biochemistry. 2004 Jun 15;43(23):7637-42. [Content Brief]

[13]. Ronald A Albright, et al. Molecular basis of purinergic signal metabolism by ectonucleotide pyrophosphatase/phosphodiesterases 4 and 1 and implications in stroke. J Biol Chem. 2014 Feb 7;289(6):3294-306. [Content Brief]

[14]. Masahiko Nishizaki, et al. Synergistic tumor suppression by coexpression of FHIT and p53 coincides with FHIT-mediated MDM2 inactivation and p53 stabilization in human non-small cell lung cancer cells. Cancer Res. 2004 Aug 15;64(16):5745-52. [Content Brief]

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