SULT1A1

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Sulfotransferase 1A1
Identifiers
EC number2.8.2.1
CAS number9029-99-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO


Sulfotransferase 1A1 (SULT1A1) is an enzyme that in humans is encoded by the SULT1A1 gene. This enzyme belongs to the family of sulfotransferases, which are responsible for the sulfation of various molecules, including hormones, neurotransmitters, drugs, and xenobiotic compounds. Sulfation is a crucial phase II metabolic process that enhances the solubility of compounds, facilitating their excretion from the body.

Structure[edit | edit source]

SULT1A1 is a cytosolic enzyme that is predominantly expressed in the liver, but it is also found in other tissues such as the intestine, lung, and brain. The enzyme is composed of a single polypeptide chain and functions as a homodimer. Each monomer of SULT1A1 contains a PAPS (3'-phosphoadenosine-5'-phosphosulfate) binding site, which is essential for its sulfotransferase activity.

Function[edit | edit source]

SULT1A1 catalyzes the transfer of a sulfonate group from PAPS to a hydroxyl or amine group of a substrate, resulting in the formation of a sulfated product. This reaction is important for the metabolism and detoxification of endogenous compounds such as estrogens and thyroid hormones, as well as exogenous compounds including drugs and environmental toxins.

Clinical Significance[edit | edit source]

Variations in the SULT1A1 gene can lead to differences in enzyme activity among individuals, affecting drug metabolism and response. Polymorphisms in SULT1A1 have been associated with altered risk for certain diseases, including breast cancer and endometrial cancer. Understanding these genetic variations is important for pharmacogenomics and personalized medicine.

Research and Applications[edit | edit source]

SULT1A1 is a subject of ongoing research due to its role in drug metabolism and its potential impact on drug efficacy and toxicity. Studies are focused on understanding the enzyme's substrate specificity, regulation, and the effects of genetic polymorphisms on its activity.

Also see[edit | edit source]

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Contributors: Prab R. Tumpati, MD