MOCOS : molybdenum cofactor sulfurase
Description
The MOCOS (molybdenum cofactor sulfurase) is a protein-coding gene located on chromosome 18.
The MOCOS gene instructs the production of an enzyme called molybdenum cofactor sulfurase. This enzyme is essential for the proper function of two other enzymes: xanthine dehydrogenase and aldehyde oxidase. Xanthine dehydrogenase plays a role in the breakdown of purines, which are components of DNA and RNA. It specifically catalyzes the conversion of hypoxanthine to xanthine and then xanthine to uric acid, a waste product excreted in urine and feces. While less is known about aldehyde oxidase, it appears to be involved in the metabolism of various compounds. Molybdenum cofactor sulfurase performs a chemical reaction that attaches a sulfur atom to a molecule called the molybdenum cofactor. This cofactor is necessary for the activation of xanthine dehydrogenase and aldehyde oxidase, allowing them to perform their functions.
The MOCOS gene product, molybdenum cofactor sulfurase (MCS), is responsible for adding a sulfur atom to the molybdenum cofactor. This sulfation process is crucial for the activation of xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes. In these enzymes, the molybdenum cofactor is bound to one oxygen and one sulfur atom in its active form. Additionally, the C-terminal domain of MCS has been shown to reduce N-hydroxylated prodrugs, such as benzamidoxime, in laboratory settings.
MOCOS is also known as HMCS, MCS, MOS.
