2-phosphosulfolactate phosphatase

2-phosphosulfolactate phosphatase is a Mg2+-dependent enzyme belonging to the hydrolase family, specifically acting on phosphoric monoester bonds (EC 3.1.3.71). It catalyzes the hydrolysis of (2R)-2-phospho-3-sulfolactate to produce (2R)-3-sulfolactate and phosphate. This enzyme is essential in the biosynthetic pathway for coenzyme M, the terminal methyl carrier in methanogenesis, particularly in methanogenic archaea such as Methanococcus jannaschii. The enzyme (also known as ComB phosphatase) is highly specific for 2-hydroxycarboxylic acid phosphate esters, requires Mg2+ for activity, exhibits a low pH optimum, and is thermostable. Homologs exist across cyanobacteria, bacteria, and archaea, often repurposed into various metabolic pathways. There is currently no clear evidence this enzyme serves as a direct therapeutic target or has characterized drug interactions or safety concerns in humans.

Other names

(R)-2-phospho-3-sulfolactate phosphohydrolaseComB phosphatase(2R)-phosphosulfolactate phosphohydrolase