Phosphoadenylylsulfatase

Phosphoadenylylsulfatase

Phosphoadenylylsulfatase is an enzyme that catalyzes the hydrolysis of 3'-phosphoadenylyl sulfate (PAPS) to adenosine monophosphate (AMP) and sulfate. This reaction is important in the metabolism of sulfur-containing compounds.

Function

Phosphoadenylylsulfatase plays a crucial role in the sulfate assimilation pathway, which is essential for the biosynthesis of sulfur-containing compounds such as cysteine and methionine. The enzyme's activity helps regulate the levels of activated sulfate in the cell, which is necessary for various sulfation reactions.

Mechanism

The enzyme catalyzes the hydrolysis of the phosphoanhydride bond in 3'-phosphoadenylyl sulfate, resulting in the formation of AMP and free sulfate. This reaction is a key step in the sulfur cycle and is important for maintaining cellular sulfur homeostasis.

Clinical Significance

Deficiencies or malfunctions in phosphoadenylylsulfatase can lead to disruptions in sulfur metabolism, which may contribute to various metabolic disorders. Understanding the enzyme's function and regulation can provide insights into potential therapeutic targets for these conditions.

See Also

• Sulfate assimilation
• Sulfur metabolism
• Enzyme catalysis

References

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External Links

• [Phosphoadenylylsulfatase at the US National Library of Medicine Medical Subject Headings (MeSH)](https://meshb.nlm.nih.gov/record/ui?name=Phosphoadenylylsulfatase)