Issue 5, 1984

β-Hydroxydecanoylthioester dehydrase. Steric course at substrate C-2 and overall steric course of the enzyme–catalysed allylic rearrangement

Abstract

β-Hydroxydecanoylthioester dehydrase (Escherichia coli)catalyses the addition of a proton to the si face at C-2 of the N-acetylcysteinamine thioester of E-dec-2-enoic acid in isomerzing this substance to the corresponding Z-dec-3-enoic acid thioester with the result that the overall steric course of the allylic rearrangement is suprafacial.

Article information

Article type
Paper

J. Chem. Soc., Chem. Commun., 1984, 298-299

β-Hydroxydecanoylthioester dehydrase. Steric course at substrate C-2 and overall steric course of the enzyme–catalysed allylic rearrangement

J. M. Schwab and J. B. Klassen, J. Chem. Soc., Chem. Commun., 1984, 298 DOI: 10.1039/C39840000298

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