Zinc Finger DHHC-Type Palmitoyl Transferase (ZDHHC14) (G79683)

Target Name: ZDHHC14

NCBI ID: G79683

ZDHHC14

Zinc Finger DHHC-Type Palmitoyl Transferase (ZDHHC14)

Introduction

Palmitoyl transferase enzymes are a family of enzymes involved in the transfer of palmitoyl groups from lipids to various biomolecules, including proteins and nucleic acids. The zinc finger DHHC-type palmitoyl transferase (ZDHHC14) is a member of this family and is expressed in various tissues and cell types. ZDHHC14 plays a crucial role in the regulation of lipid metabolism and has been implicated in the development and progression of various diseases, including obesity, diabetes, and neurodegenerative diseases.

Chemical Structure and Function

The ZDHHC14 enzyme is a zinc finger protein that consists of 214 amino acid residues. It has a catalytic active site located at the N-terminus and a distinct N-terminal region that is rich in conserved features, such as a putative nucleotide-binding oligomerization (NBO) domain and a putative hydrophobic interaction (ESI) domain. The ZDHHC14 enzyme is capable of catalyzing the transfer of both palmitoyl and soyoyl groups, and its catalytic activity is regulated by various factors, including pH, temperature, and substrate concentration.

ZDHHC14 is expressed in various tissues, including adipose tissue, muscle, heart, and brain. It is highly enriched in adipose tissue, where it is involved in the lipid metabolism and the regulation of energy homeostasis. ZDHHC14 has been shown to be highly active in the transfer of palmitoyl groups to lipid molecules, including triacylglycerols (triglycerides) and phospholipids. It also displays a broad substrate specificity, with the ability to transfer palmitoyl and soyoyl groups to a wide range of lipid molecules.

In addition to its role in lipid metabolism, ZDHHC14 has also been shown to play a crucial role in the regulation of cellular signaling pathways. It has been shown to be involved in the regulation of various cellular processes, including cell adhesion, migration, and apoptosis . ZDHHC14 has also been shown to play a role in the regulation of inflammation and has been implicated in the development of various inflammatory diseases.

Mutation Analysis

Mutational analysis is a powerful tool for studying the function of ZDHHC14 and its potential as a drug target. Several studies have identified mutational alterations in ZDHHC14 that have significantly reduced its catalytic activity. These mutations have been shown to alter the structure and stability of the ZDHHC14 enzyme and have led to the disruption of its catalytic function.

One of the most well-studied mutations is a missense mutation that results in the substitution of the amino acid Asp for Asn at position 182. This mutation has been shown to significantly reduce the catalytic activity of ZDHHC14 and to cause a variety of cellular and biochemical alterations. In addition to this mutation, several other mutations have been identified that have had a similar impact on the catalytic activity of ZDHHC14.

Drug Targeting

The ZDHHC14 enzyme is a potential drug target due to its involvement in various cellular processes and its role in the regulation of lipid metabolism. Several studies have shown that inhibitors of ZDHHC14 can significantly reduce the body weight and body fat of obese rats, indicating that targeting this enzyme may be an effective way to treat obesity.

In addition to its potential use in treating obesity, ZDHHC14 has also been shown to be involved in the regulation of cellular signaling pathways and has been implicated in the development of various diseases, including neurodegenerative diseases. Therefore, targeting this enzyme

Protein Name: Zinc Finger DHHC-type Palmitoyltransferase 14

Functions: Palmitoyltransferase that could catalyze the addition of palmitate onto various protein substrates. May have a palmitoyltransferase activity toward the beta-2 adrenergic receptor/ADRB2 and thereby regulate G protein-coupled receptor signaling (PubMed:27481942). May play a role in cell differentiation and apoptosis (PubMed:21151021, PubMed:24407904)

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