ZNG1B: A Potential Drug Target and Biomarker for Cobalamin Synthesis

Target Name: ZNG1B

NCBI ID: G150472

ZNG1B

ZNG1B: A Potential Drug Target and Biomarker for Cobalamin Synthesis

Abstract:

Cobalamin, also known as vitamin B12, is a crucial nutrient for the maintenance of cellular health and a strong immune system. It plays a vital role in the synthesis of DNA, RNA, and proteins, making it an essential factor in cellular growth and development . The cobalamin synthesis pathway is complex and involves multiple enzymes, including ZNG1B (Zinc Finger N-Glycosylating). In this article, we discuss the ZNG1B protein, its function in cobalamin synthesis, and its potential as a drug target or biomarker.

Introduction:

Cobalamin, also known as vitamin B12, is a small molecule that plays a vital role in the synthesis of DNA, RNA, and proteins. It is essential for the maintenance of cellular health and a strong immune system. Cobalamin works by participating in the cobalamin synthesis pathway, a complex process that involves the participation of multiple enzymes. One of these enzymes is ZNG1B (Zinc Finger N-Glycosylating), which is a key player in the synthesis of cobalamin.

ZNG1B: A Critical Enzyme in Cobalamin Synthesis

ZNG1B is a protein that belongs to the N-glycosylating enzyme family 1 (NGESF1) and is responsible for the N-glycosylation of the protein ZNF2 (Zinc Finger N-Glycosylating 2). ZNF2 is a key regulator of the myelination process, which is critical for the development and maintenance of the central nervous system (CNS). ZNG1B is a critical enzyme in the cobalamin synthesis pathway, as it catalyzes the final step in the synthesis of cobalamin from its precursor, mena-CoA.

Cobalamin Synthesis: A Complex Process

The cobalamin synthesis pathway is a complex process that involves multiple enzymes, including ZNG1B. The first step in the pathway is the synthesis of mena-CoA, which is a precursor to cobalamin. Mena-CoA is produced from the amino acids alanine, aspartic acid , glutamic acid, and pyruvate via the shikimate pathway. The second step in the pathway is the synthesis of the amino acid cysteine, which is also a precursor to cobalamin. Cysteine 鈥嬧?媔s produced from the amino acid homocysteine 鈥嬧?媣ia the cysteine 鈥嬧?媠ynthesis pathway.

ZNG1B: A Key Enzyme in the Cobalamin Synthesis Pathway

ZNG1B is a key enzyme in the cobalamin synthesis pathway, as it catalyzes the final step in the synthesis of cobalamin from its precursor, mena-CoA. ZNG1B is a NGESF1 enzyme, which means that it has a conserved N-glycosylation site in its protein sequence. This N-glycosylation site is critical for the stability and function of ZNG1B, as it allows the protein to interact with other proteins and substrates.

NGESF1 Enzymes:

NGESF1 is a family of N-glycosylating enzymes that plays a crucial role in the regulation of cellular processes, including cell adhesion, migration, and signaling pathways. The NGESF1 enzymes are involved in the formation of a wide range of cell surface molecules, including adhesion molecules, glycophores, and signaling molecules. ZNG1B is a member of the NGESF1 family and is responsible for the N-glycosylation of the protein ZNF2 (Zinc Finger N-Glycosylating 2).

Drug Targeting and Biomarkers

The ZNG1B protein is a potential drug target and biomarker for cobalamin synthesis disorders. Cobalamin synthesis disorders are a group of inherited disorders that are characterized by defects in the cobalamin synthesis pathway. These disorders include methylmalonyl-CoA mutase (MMCM), cobalamin deficiency, and primary cobalaminuria.

MMCM is an inherited disorder that is characterized by defects in the enzyme Mena-CoA mutase (

Protein Name: Zn Regulated GTPase Metalloprotein Activator 1B

Functions: Zinc chaperone that directly transfers zinc cofactor to target metalloproteins, thereby activating them. Catalyzes zinc insertion into the active site of methionine aminopeptidase METAP1, which function to cleave the initiator methionine from polypeptides during or after protein translation. Mechanistically, the N-terminal psi-PxLVp motif binds to the C6H2-type zinc finger of inactive form of METAP1. After formation of the docked complex, zinc is transferred from the CXCC motif in the GTPase domain of ZNG1B to the zinc binding site in the peptidase domain of METAP1 in a process requiring GTP hydrolysis. GTP/GDP exchange is required for release of active METAP1

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