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. 1977 Sep 1;165(3):575–580. doi: 10.1042/bj1650575

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

B Bartholomew, K S Dodgson, G W Matcham, D J Shaw, G F White
PMCID: PMC1164941  PMID: 921766

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.

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Selected References

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  1. DODGSON K. S. Determination of inorganic sulphate in studies on the enzymic and non-enzymic hydrolysis of carbohydrate and other sulphate esters. Biochem J. 1961 Feb;78:312–319. doi: 10.1042/bj0780312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Dickinson F. M., Dalziel K. The specificities and configurations of ternary complexes of yeast and liver alcohol dehydrogenases. Biochem J. 1967 Jul;104(1):165–172. doi: 10.1042/bj1040165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dodgson K. S., Fitzgerald J. W., Payne W. J. Chemically defined inducers of alkylsulphatases present in Pseudomonas C12B. Biochem J. 1974 Jan;138(1):53–62. doi: 10.1042/bj1380053. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fitzgerald J. W. Secondary alkylsulphatases in a strain of Comamonas terrigena. Biochem J. 1975 Aug;149(2):477–480. doi: 10.1042/bj1490477. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. HILMOE R. J., HEPPEL L. A., SPRINGHORN S. S., KOSHLAND D. E., Jr Cleavage point during hydrolyses catalyzed by ribonuclease and phosphodiesterase. Biochim Biophys Acta. 1961 Oct 14;53:214–215. doi: 10.1016/0006-3002(61)90809-5. [DOI] [PubMed] [Google Scholar]
  6. Heller M., Mozes N., Maes E. Phospholipase D from peanut seeds. EC 3.1.4.4 phosphatidylcholine phosphatidohydrolase. Methods Enzymol. 1975;35:226–232. doi: 10.1016/0076-6879(75)35158-6. [DOI] [PubMed] [Google Scholar]
  7. KOSHLAND D. E., Jr, SPRINGHORN S. S. Mechanism of action of 5'-nucleotidase. J Biol Chem. 1956 Jul;221(1):469–476. [PubMed] [Google Scholar]
  8. Mayers G. L., Pousada M., Haines T. H. Microbial sulfolipids. 3. The disulfate of (+)-1,14-docosanediol in Ochromonas danica. Biochemistry. 1969 Jul;8(7):2981–2986. doi: 10.1021/bi00835a045. [DOI] [PubMed] [Google Scholar]
  9. Pontremoli S., Traniello S., Luppis B., Wood W. A. Fructose diphosphatase from rabbit liver. I. Purification and properties. J Biol Chem. 1965 Sep;240(9):3459–3463. [PubMed] [Google Scholar]
  10. Rosenberry T. L. Acetylcholinesterase. Adv Enzymol Relat Areas Mol Biol. 1975;43:103–218. doi: 10.1002/9780470122884.ch3. [DOI] [PubMed] [Google Scholar]
  11. SPENCER B. Studies on sulphatases. 20. Enzymic cleavage of aryl hydrogen sulphates in the presence of H218O. Biochem J. 1958 May;69(1):155–159. doi: 10.1042/bj0690155. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. STEIN S. S., KOSHLAND D. E. Solubilization of certain L- and D-Peptidases of hog kidney particulates. Arch Biochem Biophys. 1952 Jul;39(1):230–231. [PubMed] [Google Scholar]
  13. Sampson E. J., Vergara E. V., Fedor J. M., Funk M. O., Benkovic S. J. On the physical properties and mechanism of action of arylsulfate sulfohydrolase II from Aspergillus oryzae. Arch Biochem Biophys. 1975 Aug;169(2):372–383. doi: 10.1016/0003-9861(75)90178-2. [DOI] [PubMed] [Google Scholar]
  14. Spencer B. Studies on sulphatases. 25. The determination of BaSO(3)O by infrared spectroscopy. Biochem J. 1959 Nov;73(3):442–447. doi: 10.1042/bj0730442. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Thomas J. H., Tudball N. Studies on the enzymic degradation of L-serine O-sulphate by a rat liver preparation. Biochem J. 1967 Nov;105(2):467–472. doi: 10.1042/bj1050467. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Tudball N., Thomas P. The enzymic degradation of L-serine O-sulphate by a specific system from pig liver. Studies on the mechanism of the reaction. Biochem J. 1972 Jan;126(1):187–191. doi: 10.1042/bj1260187. [DOI] [PMC free article] [PubMed] [Google Scholar]

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