SULT

Sulfotransferase; SULT

Sulfotransferase is a transferase enzyme that catalyzes the transfer the sulfate groups, and participates in the metabolism of endogenous compounds (such as hormones, neurotransmitters) and exogenous compounds (such as drugs, environmental pollutants). Sulfotransferase is mainly located in cytoplasm and in the Golgi apparatus, which contributes to the sulfation of small molecule substrates (such as drugs, hormones, neurotransmitters) and the sulfation of macromolecules (such as peptides, proteins, lipids, and glycosaminoglycans), respectively. Sulfotransferase have been identified into multiple subfamilies, mainly including SULT1, SULT2, and SULT4. Sulfotransferase dysfunction would lead to abnormal drug metabolism, cancer, endocrine diseases and neurological diseases^[1]^[2].

References:

[1]. Gamage N, et al., Human sulfotransferases and their role in chemical metabolism. Toxicol Sci. 2006 Mar;90(1):5-22. [Content Brief]

[2]. Chapman E, et al., Sulfotransferases: structure, mechanism, biological activity, inhibition, and synthetic utility. Angew Chem Int Ed Engl. 2004 Jul 5;43(27):3526-48. [Content Brief]

SULT Inhibitor (1)

SULT Related Products (2):

Cat. No.	Product Name	Effect	Purity	Chemical Structure

HY-124704

Chst15-IN-1	Inhibitor	98.09%
Chst15-IN-1 is a potent reversible covalent Chst15 inhibitor. Chst15-IN-1 effectively inhibits chondroitin sulfate-E (CS-E) sulfation levels and other closely related glycosaminoglycans (GAG) sulfotransferases. Chst15-IN-1, as a selective sulfotransferase inhibitor, can diminish the inhibitory effects of chondroitin sulfate proteoglycans (CSPGs), and can be used for the stimulation of neuronal repair.

HY-E70166

Carbohydrate Sulfotransferase 6
Carbohydrate Sulfotransferase 6 (EC:2.8.2.21) can catalyze sulphate transfer to position 6 of non-reducing GlcNAc residues of keratan.

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