A novel mechanism of enzymic ester hydrolysis. Inversion of configuration and carbon-oxygen bond cleavage by secondary alkylsulphohydrolases from detergent-degrading micro-organisms.
The hydrolysis was studied of potassium (+)-octan-2-yl sulphate by two analogous, optically stereospecific, secondary alkylsulphohydrolases purified from two detergent-degrading micro-organisms, Comamonas terrigena and Pseudomonas C12B. Polarimetry studies have shown that (+)-octan-2-yl sulphate prepared from (+)-octan-2-ol is hydrolysed by both enzymes to yield (-)-octan-2-ol. This inversion of configuration implies that the enzymes are catalysing the scission of the C-O bond of the C-O-S linkage, a type of bond scission apparently not hitherto encountered among hydrolytic enzymes acting on ester bonds. Enzymic hydrolysis of potassium (+)-octan-2-yl sulphate in the presence of H218O and analysis of hydrolysis products for the presence of 18O has confirmed that C-O bond scission (and not O-S bond scission) occurs with both enzymes.
D001192:Arylsulfatases / Q000378:metabolism*; D006868:Hydrolysis; D008956:Models, Chemical; D000442:Octanols; D009904:Optical Rotation; D011549:Pseudomonas / Q000201:enzymology; D013429:Sulfatases / Q000378:metabolism*; D013463:Sulfuric Acid Esters
D000442:Octanols; D013463:Sulfuric Acid Esters; D013429:Sulfatases; D001192:Arylsulfatases