Sterol esterase (StE) (StE)

Microbial sterol esterases (EC 3.1.1.13) are enzymes produced by various bacteria, fungi, and yeasts that catalyze the hydrolysis of sterol esters into free sterols and fatty acids, as well as the reverse esterification reaction [UniProt: EC 3.1.1.13]. These enzymes are essential for maintaining sterol homeostasis and mobilizing lipid stores, which are critical for nutrient acquisition and membrane integrity in microorganisms [PubMed: 25650353]. In pathogenic organisms such as Mycobacterium tuberculosis and Candida albicans, sterol esterases act as virulence factors that facilitate host tissue invasion and immune evasion by manipulating host lipid signaling pathways [PubMed: 15659397]. Consequently, they are investigated as potential therapeutic targets for novel antimicrobial agents aimed at disrupting lipid metabolism [PubMed: 28435087]. Beyond their role in pathogenesis, microbial sterol esterases are widely used in clinical diagnostics as reagents for the enzymatic determination of cholesterol levels in human serum [BRENDA: EC 3.1.1.13]. Therapeutic challenges include achieving high selectivity to avoid the inhibition of human orthologs like pancreatic cholesterol esterase, which could lead to gastrointestinal side effects and malabsorption [PubChem: Orlistat].

Other names

Cholesterol esteraseSteryl-ester acylhydrolaseCholesterol ester hydrolaseMicrobial cholesterol esterase

Covalent inhibition of the active-site serine residue, preventing the hydrolysis of sterol esters and disrupting microbial lipid metabolism.