重组人 NUDT16 蛋白 (His tag N-Terminus)
Recombinant Human NUDT16 protein (His tag N-Terminus)
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(2 Publications)
Recombinant Human NUDT16 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 195 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
查看别名
U8 snoRNA-decapping enzyme, IDP phosphatase, Inosine diphosphate phosphatase, Nucleoside diphosphate-linked moiety X motif 16, Nudix hydrolase 16, U8 snoRNA-binding protein H29K, m7GpppN-mRNA hydrolase, IDPase, Nudix motif 16, NUDT16
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human NUDT16 protein (His tag N-Terminus) (AB103059)
15% SDS-PAGE (3 μg)
反应性数据
序列信息
性能和储存信息
运输条件
推荐的短期储存时间
推荐的短期储存条件
推荐的长期储存条件
分装信息
储存信息
补充信息
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
NUDT16 functions to regulate nucleotide metabolism. It catalyzes the hydrolysis of nucleoside diphosphates like diadenosine tetraphosphate into monophosphates. NUDT16 often operates with other proteins in multi-enzyme complexes where it plays a role in modulating the concentrations of nucleoside diphosphates within cells. This activity coordinates the synthesis and degradation of nucleotides influencing cellular energy status and coenzyme levels.
Pathways
With regards to pathways NUDT16 integrates into nucleotide catabolism and salvage pathways. These pathways facilitate the conversion and recycling of nucleotides ensuring a steady supply for nucleic acid synthesis. NUDT16 interacts within these pathways alongside other key enzymes such as IMP dehydrogenase and GMP synthetase highlighting its role in controlling guanine nucleotide levels. This involvement provides a direct link to DNA replication and repair mechanisms which depend on the accurate control of nucleotide pools.
特殊说明
形式
Liquid
附加说明
ab103059 was purified using conventional chromatography techniques.
常规信息
功能
RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Also catalyzes the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less efficiencies. Has broad substrate specificity with manganese or cobalt as cofactor and can act on various RNA species. Binds to the U8 snoRNA; metal is not required for RNA-binding. May play a role in the regulation of snoRNAs and mRNAs degradation. Also acts as a phosphatase; hydrolyzes the non-canonical purine nucleotides inosine diphosphate (IDP) and deoxyinosine diphosphate (dITP) as well as guanosine diphosphate (GDP), deoxyguanosine diphosphate (dGDP), xanthine diphosphate (XDP), inosine triphosphate (ITP) and deoxyinosine triphosphate (ITP) to their respective monophosphate derivatives and does not distinguish between the deoxy- and ribose forms (PubMed : 20385596, PubMed : 26121039). The order of activity with different substrates is IDP > dIDP >> GDP = dGDP > XDP = ITP = dITP (PubMed : 20385596). Binds strongly to GTP, ITP and XTP. Participates in the hydrolysis of dIDP/IDP and probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions (PubMed : 20385596). Exhibits decapping activity towards NAD-capped RNAs and FAD-capped RNAs (PubMed : 32432673). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
序列相似性
Belongs to the Nudix hydrolase family. NUDT16 subfamily.
亚细胞定位
Nucleus
靶点信息
文献 (2)
Recent publications for all applications. Explore the full list and refine your search
Nucleic acids research 52:801-815 PubMed38000390
2023
Applications
Unspecified application
Species
Unspecified reactive species
Science advances 8:eadd4253 PubMed36197986
2022
Applications
Unspecified application
Species
Unspecified reactive species
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