adenylylsulfatase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: 5'-adenylyl sulfate + H2O = AMP + 2 H+ + sulfate. [EC:3.6.2.1, RHEA:17041]

Adenylylsulfatase activity is a molecular function that refers to the enzymatic hydrolysis of adenylyl sulfate (APS) into adenosine 3',5'-bisphosphate (PAP) and sulfate. APS is a high-energy compound that serves as a sulfur donor in various metabolic pathways, including the biosynthesis of sulfolipids, sulfated glycosaminoglycans, and steroid sulfates. Adenylylsulfatase enzymes play a crucial role in regulating the intracellular levels of APS and sulfate, thereby influencing these metabolic processes. The active site of adenylylsulfatase enzymes typically contains a metal ion, such as zinc or magnesium, which is essential for catalysis. The reaction mechanism involves the nucleophilic attack of a water molecule on the sulfur atom of APS, facilitated by the metal ion. This results in the cleavage of the sulfur-oxygen bond and the release of sulfate. The hydrolysis reaction is highly specific for APS and is not catalyzed by other sulfatases. Adenylylsulfatase activity is found in a wide range of organisms, from bacteria to humans. In humans, adenylylsulfatase deficiency is associated with various genetic disorders, including mucopolysaccharidosis type VI (Maroteaux-Lamy syndrome), which is characterized by skeletal abnormalities and intellectual disability. Understanding the molecular function of adenylylsulfatase activity is crucial for developing therapeutic strategies for these disorders.'
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Proteins (1)

Compounds (2)