nucleoside

Purine nucleoside phosphorylase (PNP) is a purine-metabolizing enzyme that catalyzes the reversible phosphorolysis of 6-oxypurine (deoxy)nucleosides to their respective bases and (deoxy)ribose-1-phosphate. It is a key enzyme in the purine salvage pathway of mammalian cells. Purine nucleoside phosphorylase is a transferase that catalyzes the addition of phosphate and removal of a purine base from guanosine and similar nucleosides.PNP defects result in metabolic abnormalities and fatal T cell immunodeficiency. Purine nucleoside phosphorylase (PNP) is a target for leukemia, gout, and autoimmune disorders.

NME4 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 44.3 kDa and the accession number is O00746.

Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Required for repair of UV radiation- and etoposide-induced DNA damage. NDPK Protein, S. cerevisiae, Recombinant (E. coli, His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 21.2 kDa and the accession number is P36010.

Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Required for repair of UV radiation- and etoposide-induced DNA damage. NDPK Protein, S. cerevisiae, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 19.2 kDa and the accession number is P36010.

NDK, cytosolic Protein, Dictyostelium discoideum, Recombinant (His & V5) is expressed in E. coli.

DCP2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 48.4 kDa and the accession number is Q8IU60.

NUDT1 (Nudix Hydrolase 1) is a Protein Coding gene. The protein encoded by this gene is an enzyme that hydrolyzes oxidized purine nucleoside triphosphates to monophosphates, thereby preventing misincorporation. The NUDT1 protein is localized mainly in the cytoplasm, with some in the mitochondria, suggesting that it is involved in the sanitization of nucleotide pools both for nuclear and mitochondrial genomes. Cancers can survive the oxidative conditions by upregulating nucleoside diphosphate linked moiety X-type motif 1 (NUDT1). MiR-485-5p acts as a tumor suppressor by targeting NUDT1 in gastric cancer (GC). The miR-485-5p/NUDT1 axis is involved in the processes of cell growth and cell motility and plays a key role in the tumorigenesis of GC.

NUDT2 Protein, Human, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 18.3 kDa and the accession number is P50583.

NUDT5 (Nudix Hydrolase 5) is a Protein Coding gene. This gene belongs to the Nudix (nucleoside diphosphate linked moiety X) hydrolase superfamily. The encoded enzyme catalyzes the hydrolysis of modified nucleoside diphosphates. ADP-sugar Pyrophosphatase, also known as NUDT5, eliminates toxic nucleotide derivatives from the cell and regulates the levels of important signaling nucleotides and their metabolites. It is widely expressed in the liver, skin, and other tissues. NUDT5 functions as a MutT-related protein and catalyzes the hydrolysis of 8-oxoGDP to 8-oxoGMP, thereby preventing misincorporation of 8-oxoGua into RNA. NUDT5 may play significant roles in regulating the G1-S transition in mammalian cells. It can also hydrolyze other nucleotide sugars with low activity.

NME1, also known as Nucleoside Diphosphate Kinase A (NDK-A), or NM23-H1, belongs to the NDK family. NM23-H1 is known to have a metastasis suppressive activity in many tumor cells. Recent studies have shown that the interacting proteins with NM23-H1 which mediate cell proliferation, may act as modulators of the metastasis suppressor activity. The interacting proteins with NM23-H1 can be classified into 3 groups. The first group of proteins can be classified as upstream kinases of NM23-H1 such as CKI and Aurora-A/STK15. The second group of proteins acts as downstream effectors for the regulation of specific gene transcriptions, GTP-binding protein functions, and signal transduction in the Erk signal cascade. The third group of proteins can be classified as bi-directionally influencing binding partners of NM23-H1. As a result, the interactions with NM23-H1 and binding partners have implications in the biochemical characterization involved in metastasis and tumorigenesis. NDKA is increased in human postmortem cerebrospinal fluid (CSF), a model of global brain insult, suggesting that measurement in CSF and, more importantly, in plasma may be useful as a biomarker of stroke. Additionally, NM23-H1 significantly reduces metastasis without effects on primary tumor size and was the first discovered metastasis suppressor gene.

Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Plays a role in response to reactive oxygen species (ROS) stress. NDK1 Protein, Arabidopsis thaliana, Recombinant (His & Myc) is expressed in yeast with N-10xHis and C-Myc tag. The predicted molecular weight is 20.5 kDa and the accession number is P39207.

NME2 Protein, Human, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 24.2 kDa and the accession number is P22392.

Inosine Triphosphate Pyrophosphatase (ITPase) is a cytoplasmic enzyme that belongs to the HAM1 NTPase family. ITPase hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP) and deoxyinosine triphosphate (dITP) to the monophosphate nucleotide (IMP) and diphosphate. The ITPase enzyme acts as a homodimer and does not distinguish between the deoxy- and ribose forms. ITPase probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions. Defects in ITPase is thought to be inherited and is characterized by an over-accumulation of ITP in erythocytes, leukocytes and fibroblasts.

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity. UMP-CMP kinase/CMPK1 Protein, Mouse, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 38.2 kDa and the accession number is Q9DBP5.

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.

In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation by hydrolyzing platelet-activating ADP to AMP. Hydrolyzes ATP and ADP equally well.

Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP)-1 is a membrane-bound protein that catalyzes the hydrolysis of extracellular nucleoside triphosphates to monophosphate and extracellular inorganic pyrophosphate (ePPi). Mechanical stimulation regulates ENPP-1 expression. ENPP1 Protein, Human, Recombinant (C-His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 96.5 kDa and the accession number is P22413.

Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP)-1 is a membrane-bound protein that catalyzes the hydrolysis of extracellular nucleoside triphosphates to monophosphate and extracellular inorganic pyrophosphate (ePPi). Mechanical stimulation regulates ENPP-1 expression. ENPP1 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 98.29 kDa and the accession number is P22413.

CD39L1 protein (ENTPD2 or NTPDase2) is a member of the ecto-nucleoside triphosphate diphosphohydrolase family which the main role is termination of purinergic signaling. CD39L1 gene encodes a precursor protein with 495 amino acid residues which generates a 437 amino acid residues mature protein after processing. It is an ecto-nucleotidase that found on the surface of vascular adventitial cells and accessory vascular cells. CD39L1 is a Ca2+- and Mg2+-dependent enzyme that activates platelets by preferentially converting ATP to ADP. CD39L1 plays a role in regulating thrombosis and inflammation which is considered to be a therapeutic target for thromboregulation and the treatment of vascular inflammation. Alternative splicing of CD39L1 gene results in multiple transcript variants.

Deoxycytidine Kinase (DCK) is a member of the DCK/DGK family. DCK exists as a homodimer and is localized to the nucleus. DCK is required for the phosphorylation of the deoxyribonucleosides deoxycytidine (dC), deoxyguanosine (dG), and deoxyadenosine (dA). DCK has broad substrate specificity, and does not display selectivity based on the chirality of the substrate. In addition, DCK is also an essential enzyme for the phosphorylation of numerous nucleoside analogs widely employed as antiviral and chemotherapeutic agents. DCK is clinically important because of its relationship to drug resistance and sensitivity.

Phosphoglucomutase-2 (PGM2) is a member of PGM family, which catalyzes the inter-conversion of sugar phosphates and participates in anabolic and catabolic reactions. When cells are grown in glucose, PGM catalyzes the conversion of glucose-6-phosphate to glucose-1-phosphate an important precursor required for the synthesis of UDP glucose and trehalose. PGM2 catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses, and it may also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. But this protein has low glucose 1,6-bisphosphate synthase activity.

Phosphorylates deoxyguanosine and deoxyadenosine in the mitochondrial matrix, with the highest efficiency for deoxyguanosine. In non-replicating cells, where cytosolic dNTP synthesis is down-regulated, mtDNA synthesis depends solely on DGUOK and TK2. Phosphorylates certain nucleoside analogs. Widely used as target of antiviral and chemotherapeutic agents.

BPHL is a member of the serine protease family. BPHL is expressed large quantities in liver and kidney and in minor quantities in heart, intestine and skeletal muscle. BPHL is a specific alpha-amino acid ester hydrolase that prefers small, hydrophobic, and aromatic side chains and does not have a stringent requirement for the leaving group other than preferring a primary alcohol. It catalyzes the hydrolytic activation of amino acid ester prodrugs of nucleoside analogs such as valacyclovir and valganciclovir. BPHL also activates valacyclovir to acyclovir. It may play a role in detoxification processes.

CMPK1 plays a key role in the maintenance of pyrimidine nucleotide pool profile and for the metabolism of pyrimidine analogs in cells. It catalyzes the phosphoryl transfer from ATP to UMP, CMP, and deoxy-CMP (dCMP), resulting in the formation of ADP and the corresponding nucleoside diphosphate. CMPK1 also has a significant role in the activation of pyrimidine analogs, which are clinically useful anti-cancer and anti-viral drugs. In the meanwhile, CMPK1 functions in cellular nucleic acid biosynthesis.

MOB-Like Protein Phocein is a member of the MOB1/Phocein Family. MOB-Like Protein Phocein is associated with membranes and the Golgi stacks. It is present in the cytosol, where it behaves as a protein complex. It has been shown that MOB-Like Protein Phocein interacts with DNM1, EPS15 and Nucleoside Diphosphate Kinase. MOB-Like Protein Phocein is the major partner of Striatin Family members and may play a important role in membrane trafficking, specifically in membrane budding reactions.

NT5C3A (5'-Nucleotidase, Cytosolic IIIA) is a Protein Coding gene. This gene encodes a member of the 5'-nucleotidase family of enzymes that catalyze the dephosphorylation of nucleoside 5'-monophosphates. The encoded protein is the type 1 isozyme of pyrimidine 5' nucleotidase and catalyzes the dephosphorylation of pyrimidine 5' monophosphates. NT5C3A expression required both an intronic IFN-stimulated response element and the IFN-stimulated transcription factor IRF1. Overexpression of NT5C3A, but not of its catalytic mutants, suppressed IL-8 production by HEK293 cells. NT5C3A-stimulated sirtuin activity resulted in deacetylation of histone H3 and the NF-kappaB subunit RelA (also known as p65), both of which were associated with the proximal region of the Il8 promoter, thus repressing the transcription of Il8 Together.

Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP)-1 is a membrane-bound protein that catalyzes the hydrolysis of extracellular nucleoside triphosphates to monophosphate and extracellular inorganic pyrophosphate (ePPi). Mechanical stimulation regulates ENPP-1 expression. ENPP1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 95.99 kDa and the accession number is P06802-1.

Ectonucleotide pyrophosphatase/phosphodiesterase (ENPP)-1 is a membrane-bound protein that catalyzes the hydrolysis of extracellular nucleoside triphosphates to monophosphate and extracellular inorganic pyrophosphate (ePPi). Mechanical stimulation regulates ENPP-1 expression. ENPP1 Protein, Human, Recombinant (N-His) is expressed in HEK293 mammalian cells with N-His tag. The predicted molecular weight is 96.5 kDa and the accession number is P22413.

Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates. Ribonuclease Protein, Bacillus amyloliquefaciens, Recombinant (His) is expressed in E. coli expression system with C-6xHis tag. The predicted molecular weight is 13.3 kDa and the accession number is P00648.

GMPR, also known as GMPR1, belongs to the IMPDH/GMPR family.This familyofenzymesincludesIMP dehydrogenaseandGMP reductase. These enzymes are involved inpurine metabolism and adopt aTIM barrelstructure. GMPR is an enzyme that catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP. GMPR functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.

NTPDase 2, also known as ENTPD2, belongs to the ecto-nucleoside triphosphate diphosphohydrolase family (E-NTPDase). Members of E-NTPDase family are nucleotidases able to hydrolyze 5′-nucleoside tri- and/or diphosphates; the main role of these enzymes is the termination of purinergic signaling. NTPDases are ubiquitous and were previously shown in other parasites including the trypanosomatides of genus Leishmania and in T. brucei. NTPase activity would act as a timer and is crucial to T. gondii infection. In L. pneumophila it was demonstrated that an E-NTPDase, similar to CD39, is essential for intracellular bacterial multiplication. NTPDase 2 is an integral membrane protein. In the nervous system, it could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Alternative splicing of NTPDase 2 gene results in multiple transcript variants.

DCTPP1 hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. It has a strong preference for modified dCTP. DCTPP1’s activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. DCTPP1 also hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). DCTPP1 does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. It may protect DNA or RNA against the incorporation of non-canonical nucleotide triphosphates. DCTPP1 may also protect cells against inappropriate methylation of CpG islands by DNA methyltransferases.