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Issue 12, 1989
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Penicillin biosynthesis: active substrates derived by methoxy substitution in the valinyl residue of the natural substrate

Abstract

The structure–reactivity profile of tripeptides modified by methoxy substitution in the valinyl moiety of L-(α-aminoadipoyl)-L-cysteinyl-D-valine with the enzyme isopenicillin N synthase has been examined; substrate bulk and absolute configuration at the oxygen-substituted carbon were found to play crucial roles in determining substrate reactivity.

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Article type: Paper
DOI: 10.1039/C39890000802
Citation: J. Chem. Soc., Chem. Commun., 1989,0, 802-804
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    Penicillin biosynthesis: active substrates derived by methoxy substitution in the valinyl residue of the natural substrate

    J. E. Baldwin, R. M. Adlington, A. Basak, P. Imming, K. Ponnamperuma, H. Ronneberg, C. J. Schofield, H. Ting and N. J. Turner, J. Chem. Soc., Chem. Commun., 1989, 0, 802
    DOI: 10.1039/C39890000802

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