Jump to main content
Jump to site search
PLANNED MAINTENANCE Close the message box

Scheduled maintenance upgrade on Thursday 4th of May 2017 from 8.00am to 9.00am (BST).

During this time our websites will be offline temporarily. If you have any questions please use the feedback button on this page. We apologise for any inconvenience this might cause and thank you for your patience.


Issue 12, 1989
Previous Article Next Article

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.

Back to tab navigation
Please wait while Download options loads

Article type: Paper
DOI: 10.1039/C39890000802
Citation: J. Chem. Soc., Chem. Commun., 1989, 802-804
  •   Request permissions

    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, 802
    DOI: 10.1039/C39890000802

Search articles by author