The Escherichia coli glucuronylsynthase promoted synthesis of steroid glucuronides: Improved practicality and broader scope

Paul Ma, Nicholas Kanizaj, Shu Ann Chan, David L. Ollis, Malcolm D. McLeod*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    10 Citations (Scopus)

    Abstract

    A library of steroid glucuronides was prepared using the glucuronylsynthase derived from Escherichia coli β-glucuronidase, followed by purification using solid-phase extraction. A representative range of steroid substrates were screened for synthesis on the milligram scale under optimised conditions with conversions dependent on steroid substitution and stereochemistry. Epiandrosterone (3β-hydroxy-5α-androstan-17-one) provided the highest conversion of 90% (84% isolated yield). The previously unreported glucuronide conjugates of methandriol (17α-methylandrost-5-ene-3β,17β-diol), cholest-5-ene-3β,25-diol and the designer steroid trenazone (17β-hydroxyestra-4,9-dien-3-one) were prepared on a multi-milligram scale suitable for characterisation by 1H and 13C NMR spectroscopy. The glucuronide conjugate of d5-etiocholanolone (2,2,3,4,4-d5-3α-hydroxy-5β-androstan-17-one), a target developed by the World Anti-Doping Agency as a certified reference material, was also prepared on a milligram scale. The improved E. coli glucuronylsynthase method provides for the rapid synthesis and purification of steroid glucuronides on a scale suitable for a range of analytical applications. This journal is

    Original languageEnglish
    Pages (from-to)6208-6214
    Number of pages7
    JournalOrganic and Biomolecular Chemistry
    Volume12
    Issue number32
    DOIs
    Publication statusPublished - 28 Aug 2014

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