ENTPD6: The Potential Drug Target for Ectonucleoside Triphosphate Diphosphohydrolase 6

Target Name: ENTPD6

NCBI ID: G955

ENTPD6: The Potential Drug Target for Ectonucleoside Triphosphate Diphosphohydrolase 6

Introduction

Ectonucleoside triphosphate diphosphohydrolase 6 (ENTPD6) is a protein that plays a crucial role in the DNA replication process in various organisms, including humans. The ENTPD6 enzyme is responsible for breaking down eukaryotic double-stranded DNA, which is crucial for the formation of a replication complex and the initiation of DNA replication. ENTPD6 is a key enzyme that enables the formation of the active form of the DNA replication complex.

Recent studies have identified ENTPD6 as a potential drug target in various diseases, including cancer, neurodegenerative diseases, and genetic disorders. The potential of ENTPD6 as a drug target is attributed to its unique mechanism of action and its involvement in multiple cellular processes.

Mechanism of Action

ENTPD6 is a nucleotide-binding enzyme that catalyzes the hydrolysis of eukaryotic double-stranded DNA at specific sites. It is composed of two subunits, alpha and beta, that are held together by a disulfide bond. The alpha subunit consists of a catalytic core and a variable region that contains the active site, where the substrate is binding takes place. The beta subunit has a nucleotide-binding domain and a carboxylic acid-exchange domain, which are responsible for the regulation of the activity of the enzyme and for the formation of the active form of the enzyme.

ENTPD6 uses a unique mechanism of action to hydrolyze DNA. It does not use ATP or GTP as substrate, but instead uses a unique triphosphate ion as a substrate. The triphosphate ion is generated by the reaction of the alpha subunit with the product of the alpha subunit cleavage of the double-stranded DNA. The alpha subunit then uses this triphosphate ion to hydrolyze the double-stranded DNA at specific sites, resulting in the formation of a single-stranded break in the double-stranded DNA.

ENTPD6 is highly specific for its target DNA sites, and the hydrolysis of DNA by ENTPD6 is dependent on the base sequence of the target site. This property makes ENTPD6 an attractive target for small molecules that can inhibit its activity.

Drug Target Potential

The potential of ENTPD6 as a drug target is attributed to its involvement in various cellular processes and its unique mechanism of action. ENTPD6 is involved in the replication process, which is a critical process for the growth and survival of cells. The inhibition of ENTPD6 activity has been shown to result in the inhibition of DNA replication, leading to the formation of cell culture resistant clones, cell death, and regression of cancer cells.

ENTPD6 is also involved in the regulation of cell growth and apoptosis. The inhibition of ENTPD6 activity has been shown to result in the inhibition of cell growth, apoptosis, and the regulation of cell cycle progression. This suggests that ENTPD6 may be a useful target for cancer therapies that involve inhibition of cell growth and apoptosis.

ENTPD6 is also involved in the regulation of inflammation and immune response. The inhibition of ENTPD6 activity has been shown to result in the inhibition of inflammation and the regulation of immune response. This suggests that ENTPD6 may be a useful target for therapies that involve the regulation of inflammation and immune response.

Conclusion

ENTPD6 is a unique and highly specific enzyme that plays a crucial role in the DNA replication process. Its involvement in various cellular processes makes it an attractive target for small molecules that can inhibit its activity. The potential of ENTPD6 as a drug target is attributed to its ability to inhibit the growth

Protein Name: Ectonucleoside Triphosphate Diphosphohydrolase 6

Functions: Catalyzes the hydrolysis of nucleoside triphosphates and diphosphates in a calcium- or magnesium-dependent manner. Has a strong preference for nucleoside diphosphates, preferentially hydrolyzes GDP, IDP, and UDP, with slower hydrolysis of CDP, ITP, GTP, CTP, ADP, and UTP and virtually no hydrolysis of ATP (PubMed:10948193, PubMed:14529283, PubMed:11041856). The membrane bound form might support glycosylation reactions in the Golgi apparatus and, when released from cells, might catalyze the hydrolysis of extracellular nucleotides (PubMed:10948193, PubMed:14529283, PubMed:11041856)

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