Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1967 Mar;102(3):929–941. doi: 10.1042/bj1020929

Inhibition of glycosidases by aldonolactones of corresponding configuration

Preparation of (1→5)-lactones by catalytic oxidation of pyranoses and study of their inhibitory properties

J Conchie 1, A J Hay 1, I Strachan 1, G A Levvy 1
PMCID: PMC1270347  PMID: 16742513

Abstract

1. A method was devised for the preparation of (1→5)-lactones from pyranose sugars and uronic acids by platinum-catalysed oxidation with gaseous oxygen in aqueous solution at acid pH. It was applied to mannose, N-acetylglucosamine, N-acetylgalactosamine, glucuronic acid, galacturonic acid, galactose, l-arabinose and d-fucose. 2. Only the first three yielded products that could be obtained in the solid state without decomposition. In every case, however, the oxidation product in aqueous solution behaved as the aldono-(1→5)-lactone, and was more inhibitory towards the appropriate glycosidases than any aldonolactone preparation hitherto examined. 3. The stabilities of the oxidation products were studied, and their interconversion with the (1→4)-lactones was demonstrated. Ring-opening does not appear to be mandatory for this isomeric change, which in some instances is very rapid. 4. To explain all the inhibitory effects observed with aldonolactones on glycosidases of corresponding configuration, it is tentatively postulated that inhibition may be due entirely to the (1→5)-lactone, and that any inhibitory effect seen with the (1→4)-lactone is a measure of the extent and speed of its conversion into the (1→5)-lactone in aqueous solution.

Full text

PDF
929

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. BITTER T., MUIR H. M. A modified uronic acid carbazole reaction. Anal Biochem. 1962 Oct;4:330–334. doi: 10.1016/0003-2697(62)90095-7. [DOI] [PubMed] [Google Scholar]
  2. CONCHIE J. Beta-Glucosidase from rumen liquor; preparation, assay and kinetics of action. Biochem J. 1954 Dec;58(4):552–560. doi: 10.1042/bj0580552. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CONCHIE J., HAY A. J. Mammalian glycosidases. 2. Properties of alpha-mannosidase and beta-galactosidase from rat epididymis. Biochem J. 1959 Oct;73:327–334. doi: 10.1042/bj0730327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. CONCHIE J., LEVVY G. A. Inhibition of glycosidases by aldonolactones of corresponding configuration. Biochem J. 1957 Feb;65(2):389–395. doi: 10.1042/bj0650389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. FINDLAY J., LEVVY G. A., MARSH C. A. Inhibition of glycosidases by aldonolactones of corresponding configuration. 2. Inhibitors of beta-N-acetylglucosaminidase. Biochem J. 1958 Jul;69(3):467–476. doi: 10.1042/bj0690467. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. FINDLAY J., LEVVY G. A. Purification of beta-N-acetylglucosaminidase from the pig epididymis. Biochem J. 1960 Oct;77:170–175. doi: 10.1042/bj0770170. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HALLIWELL G. The action of cellulolytic enzymes from Myrothecium verrucaria. Biochem J. 1961 Apr;79:185–192. doi: 10.1042/bj0790185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. HEYNS K., PAULSEN H. Selective catalytic oxidation of carbohydrates, employing plantinum catalysts. Adv Carbohydr Chem. 1962;17:169–221. doi: 10.1016/s0096-5332(08)60136-8. [DOI] [PubMed] [Google Scholar]
  9. LEVVY G. A., MARSH C. A. Synthesis of 4-methylumbelliferone beta-D-glucuronide, a substrate for the fluorimetric assay of beta-glucuronidase. Nature. 1956 Sep 15;178(4533):589–590. doi: 10.1038/178589b0. [DOI] [PubMed] [Google Scholar]
  10. LEVVY G. A., MCALLAN A. The N-acetylation and estimation of hexosamines. Biochem J. 1959 Sep;73:127–132. doi: 10.1042/bj0730127. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. LEVVY G. A., McALLAN A., HAY A. J. Inhibition of glycosidases by aldonolactones of corresponding configuration. 3. Inhibitors of beta-D-galactosidase. Biochem J. 1962 Feb;82:225–232. doi: 10.1042/bj0820225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. LEVVY G. A., McALLAN A., MARSH C. A. Purification of beta-glucuronidase from the preputial gland of the female rat. Biochem J. 1958 May;69(1):22–27. doi: 10.1042/bj0690022. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LEVVY G. A., McALLAN A. Mammalian fucosidases. 3. beta-D-Fucosidase activity and its relation to beta-D-galactosidase. Biochem J. 1963 May;87:361–367. doi: 10.1042/bj0870361. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. LEVVY G. A., McALLAN A. beta-D-Fucosidase in the Limpet, Patella vulgata. Biochem J. 1963 Apr;87:206–209. doi: 10.1042/bj0870206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. LEVVY G. A. The preparation and properties of beta-glucuronidase. IV. Inhibition by sugar acids and their lactones. Biochem J. 1952 Nov;52(3):464–472. doi: 10.1042/bj0520464. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Levvy G. A., Hay A. J., Conchie J. Inhibition of glycosidases by aldonolactones of corresponding configuration. 4. Inhibitors of mannosidase and glucosidase. Biochem J. 1964 May;91(2):378–384. doi: 10.1042/bj0910378. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. MARSH C. A., LEVVY G. A. The relationship between glucuronidase and galacturonidase activity in the limpet and in mammalian tissues. Biochem J. 1958 Apr;68(4):610–617. doi: 10.1042/bj0680610. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. PARK J. T., JOHNSON M. J. A submicrodetermination of glucose. J Biol Chem. 1949 Nov;181(1):149–151. [PubMed] [Google Scholar]
  19. TAKAHASHI T., MITSUMOTO M. TRANSFORMATION AND HYDROLYSIS OF D-GLUCONO-GAMMA AND DELTA-LACTONE. Nature. 1963 Aug 24;199:765–767. doi: 10.1038/199765a0. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES