2-phosphosulfolactate phosphatase
| 2-phosphosulfolactate phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.3.71 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a 2-phosphosulfolactate phosphatase (EC 3.1.3.71) is an enzyme that catalyzes the chemical reaction
- (2R)-2-phospho-3-sulfolactate + H2O (2R)-3-sulfolactate + phosphate
Thus, the two substrates of this enzyme are (2R)-2-phospho-3-sulfolactate and H2O, whereas its two products are (2R)-3-sulfolactate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is (R)-2-phospho-3-sulfolactate phosphohydrolase. Other names in common use include (2R)-phosphosulfolactate phosphohydrolase, and ComB phosphatase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VR0.
References
- Graham DE, Graupner M, Xu H, White RH (2001). "Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg(2+)-dependent acid phosphatases". Eur. J. Biochem. 268 (19): 5176–88. doi:10.1046/j.0014-2956.2001.02451.x. PMID 11589710.
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