MOCOS: A Critical Enzyme in Sulfur Transport and ROS Production

Target Name: MOCOS

NCBI ID: G55034

MOCOS

MOCOS: A Critical Enzyme in Sulfur Transport and ROS Production

MOCOS (Molybdenum cofactor sulfurtransferase), a protein encoded in the human gene ATP7A, is a crucial enzyme in the sulfur transport cycle of the cell. It plays a key role in the transfer of sulfur from the cell's external environment to the cell's internal organelles, including the mitochondria and endoplasmic reticulum. MOCOS is also involved in the production of reactive oxygen species (ROS), which can damage cellular components and contribute to various diseases, such as neurodegenerative disorders, cancer, and cardiovascular diseases.

The sulfur transport cycle is a complex process that involves multiple enzymes and transporters. The primary sulfur transport protein is the transport protein TTR, which is encoded in the gene ATP1A2. TTR is a nucleotide-binding protein that plays a crucial role in the binding of sulfur to the protein moiety of MOCOS. TTR functions as a nucleotide sensor and is involved in regulating the activity of MOCOS by modulating its stability.

MOCOS is a member of the superfamily of transport proteins known as the SNF (sulfur-nitrate transport factors), which includes other enzymes involved in sulfur transport, such as the bacterial enzyme SNF3 and the mouse enzyme SNF1. These enzymes share a conserved catalytic core and share similar structural features, including a nucleotide-binding domain, a transmembrane region, and a unique type of ATP-binding site.

MOCOS is a 23-kDa protein that contains 156 amino acid residues. It has a molecular weight of 41 kDa and a calculated pI of 10.9. MOCOS is highly stable and has a low expression level in various cell types, including muscle, nerve, and heart cells. It is also highly responsive to changes in pH and temperature, which suggests that it plays an important role in the regulation of cellular homeostasis.

MOCOS functions as a sulfur transport protein by transferring sulfur from the cell's external environment to its internal organelles. It does this by forming a covalent complex with TTR, which is then transported to the endoplasmic reticulum via the bloodstream. Once in the endoplasmic reticulum, MOCOS is involved in the production of ROS, which can damage cellular components and contribute to various diseases.

MOCOS is also involved in the regulation of cellular reactive oxygen species (ROS) levels. ROS are highly reactive molecules that can damage cellular components and contribute to various diseases, such as neurodegenerative disorders, cancer, and cardiovascular diseases. MOCOS plays a key role in the regulation of ROS levels by modulating the activity of other ROS-producing enzymes, such as the antioxidant NADPH oxidase (NOX) and the cytochrome P450 enzyme CYP2C9.

MOCOS is a potential drug target and biomarker for various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases. The regulation of sulfur transport and ROS production by MOCOS is a complex process that involves multiple enzymes and transporters. MOCOS has been shown to play a key role in the production of ROS, which can contribute to the development of various diseases.

In conclusion, MOCOS is a crucial enzyme involved in the sulfur transport cycle of the cell. It is a member of the SNF family of transport proteins and is involved in the transfer of sulfur from the cell's external environment to its internal organelles. MOCOS is also involved in the production of ROS, which can contribute to the development of various diseases. Therefore, MOCOS is a potential drug target and biomarker for various diseases. Further research is needed to fully understand the role of MOCOS in cellular sulfur transport and ROS production.

Protein Name: Molybdenum Cofactor Sulfurase

Functions: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. In vitro, the C-terminal domain is able to reduce N-hydroxylated prodrugs, such as benzamidoxime

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