Unlocking the Potential of NDST3: A N-deacetylase/N-sulfotransferase (HEPARAN GLUCOSAMINYL) 3 Drug Target and Biomarker

Target Name: NDST3

NCBI ID: G9348

NDST3

Unlocking the Potential of NDST3: A N-deacetylase/N-sulfotransferase (HEPARAN GLUCOSAMINYL) 3 Drug Target and Biomarker

Introduction

The heparan glucosaminyl (NGG) system is a post-translational modification of glucose in the cell, which plays a crucial role in various cellular processes, including cell signaling, adhesion, and inflammation1-3. The NGG system is composed of two main enzymes, N-deacetylase (NDAC) and N-sulfotransferase (NDST), which are involved in the modification of heparan sulfate chains4,5. In this article, we will focus on theNDST3 enzyme, also known asNDST3 (N-deacetylase/N -sulfotransferase (HEPARAN GLUCOSAMINYL) 3), as a potential drug target and biomarker in the NGG system.

NGG Modification: A Crucial Role in Cellular Processes

NGG modifications have been involved in numerous cellular processes, including cell signaling, adhesion, and inflammation. For instance, NGGS can modulate the cytoskeleton and contribute to the regulation of cell division6,7. It has also been implicated in cell adhesion, where it plays a critical role in the regulation of tight junctions and cell-cell adhesion8,9. In addition, NGGS has been linked to various signaling pathways, including the TGF-β and Wnt signaling pathways, which are involved in cell growth, differentiation, and development10 ,11.

NDST3 Enzyme: Structure and Function

NDST3 is a member of the N-sulfotransferase family, which includes other enzymes involved in post-translational modifications, such as DNA methyltransferases (DNMTs) and sulfotransferases (STS)12,13. NDST3 has a unique structure, with a catalytic domain and a distinct N-terminus that is involved in substrate recognition14,15. The catalytic domain of NDST3 consists of a Rossmann-fold, which is a common structural motif found in enzymes involved in protein-protein interactions16. The N-terminus of NDST3 contains a conserved Asp209, which is known to play a critical role in the catalytic mechanism17,18.

NDST3's Unique Structure and N-Terminal Aspartic Acid (Asp209) Helps in Substrate Recognition

The unique structure of NDST3, including its Rossmann-fold and conserved Asp209, allows it to recognize and modify specific substrates with high specificity19,20. The Rossmann-fold is a parallel beta-sheet that is formed by the alignment of the beta-strands and is responsible for the formation of a stable Rossmann-sheet-like structure. This structural motif is commonly found in proteins involved in protein-protein interactions and is known to facilitate the recognition of specific ligands16,21.

The conserved Asp209 residue in the N-terminus of NDST3 is also of particular interest, as it has been shown to play a critical role in the catalytic mechanism22,23. Asp209 is known to participate in the formation of a cation-saccharide complex, which is central to the catalytic mechanism24,25. This complex is formed upon substrate binding and is responsible for the transfer of the acetyl group from the substrate to the protein.

NGG Modification as a Potential Drug Target

The NGG system has been identified as a potential drug target in various diseases, including cancer26,27 and neurodegenerative diseases28,29. NDST3 and its associated enzymes have been shown to be involved in the modification of heparan sulfate chains, which are a key component of the NGG system30,31. The regulation of NG

Protein Name: N-deacetylase And N-sulfotransferase 3

Functions: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has high deacetylase activity but low sulfotransferase activity

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