Target intelligence / Profile preview

Nudix hydrolase 14 (NUDT14)

Target
NUDT14
Molecular classification
Enzyme, Nudix hydrolase family
01

Overview

Nudix hydrolase 14 (NUDT14) is a member of the Nudix hydrolase enzyme family that is responsible for the hydrolysis of UDP-glucose (UDPG) to glucose 1-phosphate and UMP. NUDT14 also has activity toward ADP-ribose and ADP-glucose, and can act on a limited range of nucleotide-diphosphate derivatives, but has its highest activity with UDP-glucose. By eliminating potentially toxic nucleotide metabolites and regulating the cellular availability of nucleotide substrates, NUDT14 plays a significant role in cellular metabolism and protein glycosylation pathways, such as N-glycan biosynthesis. NUDT14 shows redundancy and overlap with other Nudix enzymes, notably NUDT5, and is structurally similar to several other members of its family. Expression profiling identifies NUDT14, along with NUDT1 and NUDT5, as being upregulated in multiple cancer types, suggesting a possible, albeit not fully characterized, role in tumorigenesis and cancer metabolism. However, there are currently no known drugs or small molecules reported to directly target NUDT14, and no validated diagnostic or patient stratification biomarkers have been established for clinical use based on referenced literature. Alternative spliced transcript variants and isoforms of NUDT14 exist. There are no indications of misspelling, redundancy, or other significant informational issues in the reference nomenclature or gene data provided.

Other names
Uridine diphosphate glucose pyrophosphatase NUDT14UGPPUGPPaseUDPG pyrophosphataseNucleoside diphosphate-linked moiety X motif 14UDP-sugar diphosphatasenudix (nucleoside diphosphate linked moiety X)-type motif 14
02

Mechanism of action

Enzyme substrate hydrolysis (no known approved therapeutic inhibitors or agonists)

03

Biological functions

Regulation of nucleotide metabolite concentrationsElimination of potentially toxic nucleotide metabolitesHydrolysis of UDP-glucose to glucose 1-phosphate and UMPHydrolysis of ADP-ribose to ribose 5-phosphate and AMPProtein and mRNA expression regulation in response to metabolic demand
04

Disease associations

Cancer (highly expressed in several cancer types; potential functional relevance in cancer)Other (implicated in metabolic regulation and cellular homeostasis)
05

Safety considerations

Unclear (no specific safety concerns or therapeutic challenges reported; as with most metabolic enzymes, potential off-target metabolic impact is a theoretical consideration.)

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