Phosphoadenylylsulfatase

Phosphoadenylylsulfatase (also known as PAPS sulfatase) is an enzyme that catalyzes the hydrolysis of 3'-phosphoadenylyl sulfate (PAPS) to adenosine 3',5'-bisphosphate (PAP) and sulfate. This enzyme plays a crucial role in the sulfate activation pathway, which is essential for the biosynthesis of various sulfate esters in the body.

Function

Phosphoadenylylsulfatase is involved in the metabolism of sulfate, a process that is critical for the synthesis of various biomolecules, including proteoglycans, glycosaminoglycans, and steroid hormones. The enzyme catalyzes the conversion of PAPS, the universal sulfate donor in biological systems, to PAP and sulfate. This reaction is reversible, and the direction of the reaction depends on the relative concentrations of the substrates and products.

Structure

Phosphoadenylylsulfatase is a protein that is composed of multiple subunits. The enzyme has a complex three-dimensional structure that allows it to bind to its substrates and catalyze the reaction. The active site of the enzyme contains a magnesium ion, which is required for the catalytic activity.

Clinical significance

Mutations in the gene encoding phosphoadenylylsulfatase can lead to a rare genetic disorder known as Sulfate transporter disease. This disease is characterized by a deficiency in the enzyme, leading to an accumulation of PAPS in the body and a decrease in the synthesis of sulfate esters. Symptoms of this disease can include developmental delay, seizures, and other neurological problems.

File:Phosphoadenylylsulfatase.png

Structure of phosphoadenylylsulfatase.

See also

• Sulfate
• Enzyme
• Metabolism
• Sulfate transporter disease