NUDT14 ( 14q32.35) Elementaarit solusiivoojaentsyymit Nudixhydrolaasit

Tämä  hiiren ugp-geenin -ortologi ihmisellä UGPP   ja se kuuluu NUDIX hydrolaaseihin, joita on monta ja tämä on  NUDT14.  (Sen toiminta-aluetta on kartoitettu mm. allaolevassa  PubMed artikkelissa) .
Nudisx- hydrolaasit eliminoivat potentiellisti toksisia nukleotidimetaboliitteja solusta ja säätelevät  monien erilisten nukleotidisubstraattien, kofaktoreitten ja signaalimolekyylien   pitoisuuksia ja saatavuutta. Tämä entsyymi sisältää Nudix- hydrolaasi-domeenin ja on UDPG-pyrofosfataasi, joka hydrolysoi UDPG:n  tuottaen glukoosi-1-fosfaattia ja UMP:tä. Alternatiivisesti pleissautunueet transkriptivariantit koodaavat tämän geenin  eri isoformeja. Geeniä ilmenee rasvassa, munuaisessa ja 25 muussa kudoksessa.

• https://www.ncbi.nlm
• .nih.gov/gene/256281

• Also known as UGPP; UGPPase

• Summary

• The protein encoded by this gene is a member of the Nudix hydrolase family. Nudix hydrolases eliminate potentially toxic nucleotide metabolites from the cell and regulate the concentrations and availability of many different nucleotide substrates, cofactors, and signaling molecules. This enzyme contains a Nudix hydrolase domain and is a UDPG pyrophosphatase that hydrolyzes UDPG to produce glucose 1-phosphate and UMP. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2016]

• Expression

Ubiquitous expression in fat (RPKM 8.0), kidney (RPKM 7.1) and 25 other tissues See more

Structure, isoform 1:  (222 aminoacids) ,https://www.ncbi.nlm.nih.gov/protein/NP_803877.2
 Isoform 2:   (149 aminoacids) https://www.ncbi.nlm.nih.gov/protein/NP_001305309.1

• Conserved Domains (1) summary

cl00447
Location:39 → 145

Nudix hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue nudix motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of nudix hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the nudix hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.

 

Related articles in PubMed

1. Cloning, expression and characterization of a mammalian Nudix hydrolase-like enzyme that cleaves the pyrophosphate bond of UDP-glucose. Yagi T, et al. Biochem J, 2003 Mar 1. PMID 12429023, Free PMC Article
2. Human cytomegalovirus RL13 protein interacts with host NUDT14 protein affecting viral DNA replication. Wang G, et al. Mol Med Rep, 2016 Mar. PMID 26781650
3. Novel raf kinase protein-protein interactions found by an exhaustive yeast two-hybrid analysis. Yuryev A, et al. Genomics, 2003 Feb. PMID 12620389
4. The DNA sequence and analysis of human chromosome 14. Heilig R, et al. Nature, 2003 Feb 6. PMID 12508121
5. Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells. Lee OH, et al. Mol Cell Proteomics, 2011 Feb. PMID 21044950, Free PMC Article

See all (11) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

Preferred Names

uridine diphosphate glucose pyrophosphatase

Names

UDP-sugar diphosphatase

UDPG pyrophosphatase

nudix (nucleoside diphosphate linked moiety X)-type motif 14

NP_001305309.1

• EC 3.6.1.45

NP_803877.2

• EC 3.6.1.45

 

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. the interaction between the RL13 protein and NUDT14 protein may be involved in human cytomegalovirus DNA replication.

Submit: New GeneRIF Correction

Huomaa tässä alla olevassa artikkelissa: 

tiivistelmä. Abstract

UDP-glukoosipyrofosfataasi on tässä työssä luonnehdittu possun munuaisesta. Tämä entsyymi hydrolysoi UDPG- rakennetta, UDP-glukoosia, joka on monen glykosylaatioreaktion edeltäjämolekyyli eläimillä ja  tuotteina on glukoosi-1-fosfaattia (Glc1P)  ja UMP:tä Sekvenssianalyyseissä tämä UGPPaasi- entsyymi  osoittautui   nukleotidi-sokerihydrolaasien tavoin olevan  jäsen yleisesti  esiintyvissä nukleotidipyrofosfataasien ryhmässä, Nudix-hydrolaasin joukossa. Täydellinen  cDNA eristettiin  UGPPaasia koodaavasta geenistä, jolle annettiin nimi UGPP.  cDNA  eristettiin kilpirauhasen cDNA-kirjastosta ja ilmennettiin E-Colissa.  Tulossolut akkumuloivat proteiinia, jolla osoittautui  olevan kineettisten ominaisuuksien identtisyydet  possun UGPPaasi- entsyymin kanssa.

• A distinct UDP-glucose (UDPG) pyrophosphatase (UGPPase, EC 3.6.1.45) has been characterized using pig kidney ( Sus scrofa ). This enzyme hydrolyses UDPG, the precursor molecule of numerous glycosylation reactions in animals, to produce glucose 1-phosphate (G1P) and UMP. Sequence analyses of the purified enzyme revealed that, similar to the case of a nucleotide-sugar hydrolase controlling the intracellular levels of ADP-glucose linked to glycogen biosynthesis in Escherichia coli [Moreno-Bruna, Baroja-Fernández, Muñoz, Bastarrica-Berasategui, Zandueta-Criado, Rodri;guez-López, Lasa, Akazawa and Pozueta-Romero (2001) Proc. Natl. Acad. Sci. U.S.A. 98, 8128-8132], UGPPase appears to be a member of the ubiquitously distributed group of nucleotide pyrophosphatases designated Nudix hydrolases. A complete cDNA of the UGPPase-encoding gene, designated UGPP, was isolated from a human thyroid cDNA library and expressed in E. coli. The resulting cells accumulated a protein that showed kinetic properties identical to those of pig UGPPase.Full Text The Full Text of this article is available as a PDF (383K).

 https://www.uniprot.org/uniprot/O95848

(Saattaa olla että tämä entsyymi  ei avusta galaktoosiaineenvaihdunnan puolella ihmisellä. ehkä jokin toinen hydrolaasi  olisi  sillä puolella.  Vasta kun galaktoosista jo on tullut  UDP-Glc, tämä entsyymi voi vaikuttaa.