Sulfatases
| Sulfatases | ||
|---|---|---|
| Enzyme classification | ||
| EC, category | 3.1.6. , Esterases | |
| Response type | hydrolysis | |
| Substrate | Sulfate ester | |
| Products | Alcohol + sulfate | |
Sulphatases are enzymes from the group of esterases that break down sulphate esters into alcohol and sulphate by hydrolysis . They can be assigned to the enzyme class EC 3.1.6.
properties
Sulphatases must first be activated before they can break bonds. Sulfatases are modified post-translationally in their active center . The enzyme FGE changes a cysteine into a formylglycine, which plays a major role in the cleavage mechanism of the sulfatases.
cleavage
When a sulfate ester is cleaved, a trans-sulfation-elimination mechanism takes place. First, the formylglycine in the active center is hydrated to form a diol . The hydroxyl group of the sulfatase can then nucleophilically attack a sulfate ester. As a result, the alcohol is split off from the sulfate ester and the sulfate is bound to the sulfatase. When the sulfate is split off from the enzyme, formylglycine is produced again.
Examples
According to current research, humans have 17 sulfatases. Most of these are located in the lysosomes . Known are:
- The aryl sulfatases aryl sulfatase A , aryl sulfatase B , aryl sulfatases CK
- Iduronate 2 sulfatase
Individual evidence
- ↑ sulfatases. Retrieved November 20, 2019 .
- ↑ Thomas Dierks, Achim Dickmanns, Andrea Preusser-Kunze, Bernhard Schmidt, Malaiyalam Mariappan: Molecular Basis for Multiple Sulfatase Deficiency and Mechanism for Formylglycine Generation of the Human Formylglycine-Generating Enzyme . In: Cell . tape 121 , no. 4 , May 20, 2005, ISSN 0092-8674 , p. 541-552 , doi : 10.1016 / j.cell.2005.03.001 , PMID 15907468 ( cell.com [accessed November 20, 2019]).
- ↑ a b Mühlhausen: Investigations on the molecular cause of the multiple sulfatase deficiency: purification, function and structure analysis of variant proteins of the formylglycine-generating enzyme. Retrieved November 20, 2019 .