CPD-1

CPD-1 or Cyclic Pyranopterin Monophosphate Synthase is an enzyme that plays a crucial role in the biosynthesis of the molybdenum cofactor (MoCo). This enzyme is encoded by the MOCS1 gene in humans.

Function

CPD-1 is involved in the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP). This is a critical step in the biosynthesis of the molybdenum cofactor (MoCo). MoCo is essential for the function of several enzymes, including sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. These enzymes play a vital role in purine catabolism, sulfite detoxification, and other metabolic processes.

Clinical significance

Mutations in the MOCS1 gene, which encodes CPD-1, can lead to a deficiency in MoCo. This deficiency is associated with a rare autosomal recessive metabolic disorder known as Molybdenum cofactor deficiency. This disorder is characterized by severe neurological damage, seizures, and early death.

Structure

The structure of CPD-1 is complex, with multiple domains that are necessary for its function. The enzyme contains a GTP-binding domain, a cPMP-synthase domain, and a molybdopterin-converting factor domain. The structure of CPD-1 has been determined using X-ray crystallography.

See also

• Molybdenum cofactor
• Molybdenum cofactor deficiency
• Enzyme
• X-ray crystallography