NUDT9

NUDT9
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1Q33, 1QVJ
Identifiers
Aliases	NUDT9 , NUDT10, nudix hydrolase 9
External IDs	OMIM: 606022 MGI: 1921417 HomoloGene: 11435 GeneCards: NUDT9
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	104,213,245 bp
RNA expression pattern
	Top expressed in
	islet of Langerhans; ; body of pancreas; ; middle temporal gyrus; ; duodenum; ; parotid gland; ; Right adrenal gland; ; rectum; ; jejunal mucosa; ; Left adrenal gland; ; glomerulus;
	Top expressed in
	saccule; ; otic placode; ; seminiferous tubule; ; sciatic nerve; ; interventricular septum; ; extensor digitorum longus muscle; ; plantaris muscle; ; supraoptic nucleus; ; utricle; ; spermatid;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	hydrolase activity ; ADP-ribose diphosphatase activity ; ADP-sugar diphosphatase activity ; adenosine-diphosphatase activity ;
Cellular component	mitochondrial matrix ; intracellular anatomical structure ; extracellular exosome ; mitochondrion ; cell junction ; nuclear membrane ;
Biological process	nucleobase-containing small molecule catabolic process ; IDP catabolic process ; ADP catabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	53343
	74167
	n/a
	ENSMUSG00000029310
	Q9BW91
	Q8BVU5
	NM_001248011 ; NM_024047 ; NM_198038
	NM_028794
	NP_001234940 ; NP_076952 ; NP_932155
	NP_083070
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

ADP-ribose pyrophosphatase, mitochondrial is an enzyme that in humans is encoded by the NUDT9 gene.^[4]^[5]^[6]

Related Research Articles

ADP-ribose diphosphatase (EC 3.6.1.13) is an enzyme that catalyzes a hydrolysis reaction in which water nucleophilically attacks ADP-ribose to produce AMP and D-ribose 5-phosphate. Enzyme hydrolysis occurs by the breakage of a phosphoanhydride bond and is dependent on Mg²⁺ ions that are held in complex by the enzyme.

Prokineticin receptor 1, also known as PKR₁, is a human protein encoded by the PROKR1 gene.

Cleavage and polyadenylation specificity factor subunit 5 (CPSF5) is an enzyme that in humans is encoded by the NUDT21 gene. It belongs to the Nudix family of hydrolases.

Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] is an enzyme that in humans is encoded by the NUDT2 gene.

Bst1 is an enzyme that in humans is encoded by the BST1 gene. CD157 is a paralog of CD38, both of which are located on chromosome 4 (4p15) in humans.

Aquaporin-7 (AQP-7) is a protein that in humans is encoded by the AQP7 gene.

Diphosphoinositol polyphosphate phosphohydrolase 3-beta is an enzyme that in humans is encoded by the NUDT11 gene.

Tankyrase-2 is an enzyme that in humans is encoded by the TNKS2 gene.

(ADP-ribosyl)hydrolase 3 (ARH3) is an enzyme that in humans is encoded by the ADPRHL2 gene (also called ADPRS). This enzyme reverses the proteins’ post-translational addition of ADP-ribose to serine residues as part of the DNA damage response The enzyme is also known to cleave poly(ADP-ribose) polymers, 1''-O-acetyl-ADP-ribose and alpha-NAD⁺

Poly [ADP-ribose] polymerase 8 is an enzyme that in humans is encoded by the PARP8 gene.

Diphosphoinositol polyphosphate phosphohydrolase 2 is an enzyme that in humans is encoded by the NUDT4 gene.

Diphosphoinositol polyphosphate phosphohydrolase 1 is an enzyme that in humans is encoded by the NUDT3 gene.

Peroxisomal NADH pyrophosphatase NUDT12 is an enzyme that in humans is encoded by the NUDT12 gene.

ADP-sugar pyrophosphatase is an enzyme that in humans is encoded by the NUDT5 gene.

Dual specificity protein phosphatase 18 is an enzyme that is encoded by the DUSP18 gene in humans.

Glyoxalase domain-containing protein 4 is an enzyme that in humans is encoded by the GLOD4 gene.

NUDIX hydrolases are a superfamily of hydrolytic enzymes capable of cleaving nucleoside diphosphates linked to x, hence their name. The reaction yields nucleoside monophosphate (NMP) plus X-P. Substrates hydrolysed by nudix enzymes comprise a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity. Enzymes of the NUDIX superfamily are found in all types of organisms, including eukaryotes, bacteria and archaea.

Ghk.

Mn²⁺-dependent ADP-ribose/CDP-alcohol diphosphatase (EC 3.6.1.53, Mn2+-dependent ADP-ribose/CDP-alcohol pyrophosphatase, ADPRibase-Mn) is an enzyme with systematic name CDP-choline phosphohydrolase. This enzyme catalyses the following chemical reaction

Nudix hydrolase 15 is a protein that in humans is encoded by the NUDT15 gene.

References

1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029310 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Perraud AL, Fleig A, Dunn CA, Bagley LA, Launay P, Schmitz C, Stokes AJ, Zhu Q, Bessman MJ, Penner R, Kinet JP, Scharenberg AM (May 2001). "ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology". Nature. 411 (6837): 595–9. Bibcode:2001Natur.411..595P. doi:10.1038/35079100. PMID 11385575. S2CID 4338852.
↑ Perraud AL, Shen B, Dunn CA, Rippe K, Smith MK, Bessman MJ, Stoddard BL, Scharenberg AM (Jan 2003). "NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase". J Biol Chem. 278 (3): 1794–801. doi: 10.1074/jbc.M205601200 . PMID 12427752.
↑ "Entrez Gene: NUDT9 nudix (nucleoside diphosphate linked moiety X)-type motif 9".

Lin S, Gasmi L, Xie Y, et al. (2002). "Cloning, expression and characterisation of a human Nudix hydrolase specific for adenosine 5'-diphosphoribose (ADP-ribose)". Biochim. Biophys. Acta. 1594 (1): 127–35. doi:10.1016/S0167-4838(01)00296-5. PMID 11825615.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Zhang HT, Yan ZQ, Hu XB, et al. (2004). "Interaction of C17orf25 with ADP-ribose pyrophosphatase NUDT9 detected via yeast two-hybrid method". Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao. 35 (8): 747–51. PMID 12897971.
Shen BW, Perraud AL, Scharenberg A, Stoddard BL (2003). "The crystal structure and mutational analysis of human NUDT9". J. Mol. Biol. 332 (2): 385–98. doi:10.1016/S0022-2836(03)00954-9. PMID 12948489.
Clark HF, Gurney AL, Abaya E, et al. (2003). "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment". Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMC 403697 . PMID 12975309.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Otsuki T, Ota T, Nishikawa T, et al. (2007). "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries". DNA Res. 12 (2): 117–26. doi: 10.1093/dnares/12.2.117 . PMID 16303743.
Carloto A, Costas MJ, Cameselle JC, et al. (2006). "The specific, submicromolar-Km ADP-ribose pyrophosphatase purified from human placenta is enzymically indistinguishable from recombinant NUDT9 protein, including a selectivity for Mn2+ as activating cation and increase in Km for ADP-ribose, both elicited by H2O2". Biochim. Biophys. Acta. 1760 (10): 1545–51. doi:10.1016/j.bbagen.2006.06.003. PMID 16860484.

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[refGRCm38Ensembl-1] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029310 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11385575-4] Perraud AL, Fleig A, Dunn CA, Bagley LA, Launay P, Schmitz C, Stokes AJ, Zhu Q, Bessman MJ, Penner R, Kinet JP, Scharenberg AM (May 2001). "ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology". Nature. 411 (6837): 595–9. Bibcode:2001Natur.411..595P. doi:10.1038/35079100. PMID 11385575. S2CID 4338852.

[pmid12427752-5] Perraud AL, Shen B, Dunn CA, Rippe K, Smith MK, Bessman MJ, Stoddard BL, Scharenberg AM (Jan 2003). "NUDT9, a member of the Nudix hydrolase family, is an evolutionarily conserved mitochondrial ADP-ribose pyrophosphatase". J Biol Chem. 278 (3): 1794–801. doi: 10.1074/jbc.M205601200 . PMID 12427752.

[entrez-6] "Entrez Gene: NUDT9 nudix (nucleoside diphosphate linked moiety X)-type motif 9".

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NUDT9

Related Research Articles

References

Further reading