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Last update 08 May 2025

NUDT13

Last update 08 May 2025

Basic Info

Synonyms

DKFZp586P2219, NAD(P)H pyrophosphatase NUDT13, mitochondrial, Nucleoside diphosphate-linked moiety X motif 13

+ [4]

Introduction

NAD(P)H pyrophosphatase that hydrolyzes NADH into NMNH and AMP, and NADPH into NMNH and 2',5'-ADP. Has a marked preference for the reduced pyridine nucleotides. Does not show activity toward NAD-capped RNAs; the NAD-cap is an atypical cap present at the 5'-end of some RNAs.

Drugs associated with NUDT13

CN117069821

Patent Mining

Target

NUDT13

Mechanism-

Active Org.

Cancer Prevention and Treatment Center of Sun Yat sen University (Affiliated Cancer Hospital of Sun Yat sen University, Cancer Research Institute of Sun Yat sen University)

Originator Org.

Cancer Prevention and Treatment Center of Sun Yat sen University (Affiliated Cancer Hospital of Sun Yat sen University, Cancer Research Institute of Sun Yat sen University)

Active Indication

Gastrointestinal Neoplasms

Inactive Indication-

Drug Highest PhaseDiscovery

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with NUDT13

100 Translational Medicine associated with NUDT13

0 Patents (Medical) associated with NUDT13

Literatures (Medical) associated with NUDT13

01 Apr 2025·Advanced Science

Nudix Hydrolase 13 Impairs the Initiation of Colorectal Cancer by Inhibiting PKM1 ADP‐Ribosylation

Article

Author: Li, Siyu ; Chen, Jiewei ; Wang, Fengwei ; Huang, Cijun ; Zou, Bingxu ; Han, Kai ; Lv, Yongrui ; Xie, Dan ; Lin, Jinlong ; Cao, Jinghua ; Chen, Yufan ; Xu, Shuidan ; Yin, Yixin

AbstractMetabolic dysregulation has been implicated as a key factor in colorectal cancer (CRC) initiation, however, the underlying driving forces and mechanisms remain poorly understood. Herein, transcriptome profiling of paired early‐stage CRCs and adenomas identifies Nudix hydrolase 13 (NUDT13) as a critical suppressor. Elevated NUDT13 expression impedes the proliferation of CRC cells under hypoxic conditions and markedly inhibits CRC initiation by upregulating PKM1. Mechanistically, NUDT13 directly binds and stabilizes PKM1 protein by reducing its poly ADP‐ribosylation (PARylation), which is catalyzed by PARP1 at E275/D281/E282/E285/D296, thereby inducing an oxidative phosphorylation (OXPHOS) phenotype in CRC cells. Moreover, spatiotemporal knockout of Nudt13 enhances intestinal tumorigenesis in mice, which can be significantly suppressed by PARP1 inhibitor Olaparib. Notably, residues E245/E248/E249 within the Nudix box motif of NUDT13 are essential for PKM1 PARylation, and a mimic peptide derived from this motif is sufficient to stabilize PKM1 protein and robustly inhibit CRC tumorigenesis. Collectively, this study reveals a previously unknown PARylation‐dependent mechanism that regulates PKM1 protein stability and switches the metabolic pathway of CRC cells, providing a promising target for CRC treatment.

01 Oct 2017·The Protein JournalQ4 · BIOLOGY

Mouse Nudt13 is a Mitochondrial Nudix Hydrolase with NAD(P)H Pyrophosphohydrolase Activity

Q4 · BIOLOGY

Article

Author: Spiller, David G ; McLennan, Alexander G ; Abdelraheim, Salama R

AbstractThe mammalian NUDT13 protein possesses a sequence motif characteristic of the NADH pyrophosphohydrolase subfamily of Nudix hydrolases. Due to the persistent insolubility of the recombinant product expressed in Escherichia coli, active mouse Nudt13 was expressed in insect cells from a baculovirus vector as a histidine-tagged recombinant protein. In vitro, it efficiently hydrolysed NADH to NMNH and AMP and NADPH to NMNH and 2′,5′-ADP and had a marked preference for the reduced pyridine nucleotides. Much lower activity was obtained with other nucleotide substrates tested. Km and kcat values for NADH were 0.34 mM and 7 s−1 respectively. Expression of Nudt13 as an N-terminal fusion to green fluorescent protein revealed that it was targeted exclusively to mitochondria by the N-terminal targeting peptide, suggesting that Nudt13 may act to regulate the concentration of mitochondrial reduced pyridine nucleotide cofactors and the NAD(P)+/NAD(P)H ratio in this organelle and elsewhere. Future studies of the enzymology of pyridine nucleotide metabolism in relation to energy homeostasis, redox control, free radical production and cellular integrity should consider the possible regulatory role of Nudt13.

22 Mar 2016·Oncotarget

Metastatic pathway-specific transcriptome analysis identifies MFSD4 as a putative tumor suppressor and biomarker for hepatic metastasis in patients with gastric cancer

Article

Author: Tanaka, Haruyoshi ; Yamada, Suguru ; Kodera, Yasuhiro ; Shibata, Masahiro ; Tanaka, Chie ; Hayashi, Masamichi ; Sugimoto, Hiroyuki ; Shimizu, Dai ; Kanda, Mitsuro ; Fujii, Tsutomu ; Fujiwara, Michitaka ; Iwata, Naoki ; Kobayashi, Daisuke ; Nakayama, Goro ; Koike, Masahiko

Gastric cancer (GC) with hepatic metastasis remains a fatal disease. Global expression profiling was conducted using tissues from patients who had GC with synchronous hepatic metastasis, and major facilitator superfamily domain containing 4 (MFSD4) was identified as a candidate biomarker for hepatic metastasis in GC. Functional and expression analyses of this molecule in GC cell lines and clinical samples were conducted. We analyzed MFSD4 expression, DNA methylation, and copy number. RNA interference experiments evaluated the effects of MFSD4 expression on cell phenotype and apoptosis. We analyzed tissues of 200 patients with GC to assess the diagnostic performance of MFSD4 levels for predicting hepatic recurrence, metastasis, or both. Differential expression of MFSD4 mRNA by GC cell lines correlated positively with the levels of NUDT13 and OCLN mRNAs and inversely with those of BMP2. Hypermethylation of the MFSD4 promoter was detected in cells with lower levels of MFSD4 mRNA. Inhibition of MFSD4 expression significantly increased the invasiveness and motility of GC cells but did not influence cell proliferation or apoptosis. MFSD4 mRNA levels in primary GC tissues were reduced in patients with concomitant hepatic metastasis or recurrence compared with those without. Low levels of MFSD4 mRNA in primary GC tissues were an independent risk factor of hepatic recurrence and metastasis. MFSD4 expression in gastric tissues may represent a useful biomarker for identification of patients at high risk for hepatic recurrence, metastasis, or both.

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NUDT13

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