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

E., Baldwin J. ; M., Adlington R. ; Basak, Amit ; P., Imming ; K., Ponnamperuma ; H., Ronneberg ; J., Schofield C. ; Ting, Hong-hoi ; J., Turner N. (1989) Penicillin biosynthesis: active substrates derived by methoxy substitution in the valinyl residue of the natural substrate Journal of the Chemical Society ,Chemical Communications (12). pp. 802-804. ISSN 0022-4936

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Official URL: http://www.rsc.org/publishing/journals/article.asp...

Related URL: http://dx.doi.org/10.1039/C39890000802

Abstract

The structure-reactivity profile of tripeptides modified by methoxy substitution in the valinyl moiety of M-(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.

Item Type:Article
Source:Copyright of this article belongs to Royal Society of Chemistry.
ID Code:1797
Deposited On:05 Oct 2010 12:00
Last Modified:13 Jan 2011 12:32

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