apyrase

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Apyrase
	structure and protein design of human apyrase
Identifiers
Symbol	Apyrase
Pfam	PF06079
InterPro	IPR009283
SCOP	1s1d
SUPERFAMILY	1s1d
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

アピラーゼ

同: CD39

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/05/15 00:11:12」(JST)

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[Wiki en表示]

Apyrase (EC 3.6.1.5, ATP-diphosphatase, adenosine diphosphatase, ADPase, ATP diphosphohydrolase) is a calcium-activated plasma membrane-bound enzyme (magnesium can also activate it) (EC 3.6.1.5) that catalyses the hydrolysis of ATP to yield AMP and inorganic phosphate. Two isoenzymes are found in commercial preparations from S. tuberosum. One with a higher ratio of substrate selectivity for ATP:ADP (approx 10) and another with no selectivity (ratio 1).

It can also act on ADP and other nucleoside triphosphates and diphosphates with the general reaction being NTP -> NDP + Pi -> NMP + 2Pi.

The salivary apyrases of blood-feeding arthropods are nucleotide hydrolysing enzymes that are implicated in the inhibition of host platelet aggregation through the hydrolysis of extracellular adenosine diphosphate.^[1]

References

^ Smith TM, Hicks-Berger CA, Kim S, Kirley TL (October 2002). "Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases". Arch. Biochem. Biophys. 406 (1): 105–15. doi:10.1016/S0003-9861(02)00420-4. PMID 12234496.

External links

Apyrase at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the public domain Pfam and InterPro IPR009283

Molecular and Cellular Biology portal

This hydrolase article is a stub. You can help Wikipedia by expanding it.

English Journal

High-throughput assays of leloir-glycosyltransferase reactions: The applications of rYND1 in glycotechnology.

Li Y1, Hou J2, Wang F3, Sheng J4.
Journal of biotechnology.J Biotechnol.2016 Jun 10;227:10-8. doi: 10.1016/j.jbiotec.2016.04.003. Epub 2016 Apr 5.
Glycosyltransferases (GTs) play a critical role in the enzymatic and chemoenzymatic synthesis of oligosaccharides and glycoconjugates. However, the development of these synthetic approaches has been limited by a lack of sensitive screening methods for the isolation of novel natural GTs or their acti
PMID 27059478

Mechanisms of NLRP3 inflammasome activation and its role in NSAID-induced enteropathy.

Higashimori A1, Watanabe T1, Nadatani Y1, Takeda S1, Otani K1, Tanigawa T1, Yamagami H1, Shiba M1, Tominaga K1, Fujiwara Y1, Arakawa T1.
Mucosal immunology.Mucosal Immunol.2016 May;9(3):659-68. doi: 10.1038/mi.2015.89. Epub 2015 Sep 9.
Nonsteroidal anti-inflammatory drugs (NSAIDs) induce cytokines, including tumor necrosis factor-α and interleukins (ILs), in the small intestine via a Toll-like receptor 4 (TLR4)-dependent pathway, leading to intestinal ulceration. Activation of the inflammasome promotes pro-caspase-1 cleavage, lea
PMID 26349656

The P2RY2 Receptor Induces Carcinoma Cell Migration and EMT Through Cross-Talk With Epidermal Growth Factor Receptor.

Martínez-Ramírez AS1, Garay E1, García-Carrancá A2,3, Vázquez-Cuevas FG1.
Journal of cellular biochemistry.J Cell Biochem.2016 Apr;117(4):1016-26. doi: 10.1002/jcb.25390. Epub 2015 Oct 14.
Extracellular nucleotides are signaling elements present in the tumor microenvironment; however, their role in tumor growth is not completely understood. In the present study, we asked whether nucleotides regulate cell migration in ovarian carcinoma-derived cells. We observed that 100 μM UTP indu
PMID 26443721

Japanese Journal

Contribution of extracellular ATP on the cell-surface F1F0-ATP synthase-mediated intracellular triacylglycerol accumulation

KITA Toshiyuki,ARAKAKI Naokatu
Biomedical Research 36(2), 115-120, 2015
… Piceatannol, a F1F0-ATP synthase inhibitor, and apyrase, an enzyme which degrades extracellular ATP, suppressed triacylglycerol accumulation. …
NAID 130005065278

植物細胞壁における病原体認識・情報伝達・応答のダイナミズム

豊田和弘,田中佳織,稲垣善茂 [他],一瀬勇規,白石友紀
日本植物病理学会報 80(3), 146-151, 2014
The plant cell wall is well known to act as a physical barrier against invading pathogens. However, our recent studies have suggested that the plant cell wall can perceive pathogen signals and is invo …
NAID 130004691243

Plant cell walls as suppliers of potassium and sodium ions for induced resistance in pea (Pisum sativum L.) and cowpea (Vigna unguiculata L.)

AMANO Masashi,TOYODA Kazuhiro,KIBA Akinori,INAGAKI Yoshishige,ICHINOSE Yuki,SHIRAISHI Tomonori
Journal of general plant pathology : JGPP 79(1), 12-17, 2013-01-01
NAID 10031145670

Related Pictures

[pmid12234496-1] Smith TM, Hicks-Berger CA, Kim S, Kirley TL (October 2002). "Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases". Arch. Biochem. Biophys. 406 (1): 105–15. doi:10.1016/S0003-9861(02)00420-4. PMID 12234496.

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