Unknown

Dataset Information

0

A novel mechanism of enzymic ester hydrolysis. Inversion of configuration and carbon-oxygen bond cleavage by secondary alkylsulphohydrolases from detergent-degrading micro-organisms.


ABSTRACT: 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.

SUBMITTER: Bartholomew B 

PROVIDER: S-EPMC1164941 | biostudies-other | 1977 Sep

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1183719 | biostudies-other
| S-EPMC9878459 | biostudies-literature
| S-EPMC1183735 | biostudies-other
| PRJEB22123 | ENA
| S-EPMC1183839 | biostudies-other
| S-EPMC1215204 | biostudies-other
| S-EPMC1137691 | biostudies-other
| S-EPMC6644415 | biostudies-literature
| S-EPMC136243 | biostudies-literature
| S-EPMC5746235 | biostudies-literature