Issue 22, 1983

Penicillin biosynthesis. On the stereochemistry of carbon–sulphur bond formation with modified substrates

Abstract

Enzymatic conversion of the two modified substrates (S-α-amino-δ-adipyl)-S-cysteinyl-(2R,3R)-3-2H-α-aminobutyrate (2c) and (S-α-amino-δ-adipyl)-S-cysteinyl-(2R,3S)-3-2H-α-aminobutyrate (2d) by the enzyme isopenicillin N synthetase gave from both precursors the same penam product, namely (2S)-2-deuterio-norisopenicillin N, indicating that this enzyme is capable of forming carbon–sulphur bonds by retention and also inversion pathways respectively.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1983, 1319-1320

Penicillin biosynthesis. On the stereochemistry of carbon–sulphur bond formation with modified substrates

J. E. Baldwin, E. P. Abraham, R. M. Adlington, J. A. Murphy, N. B. Green, H. Ting and J. J. Usher, J. Chem. Soc., Chem. Commun., 1983, 1319 DOI: 10.1039/C39830001319

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