β-Hydroxydecanoyl Thioester Dehydrase
Year: 1968
Type: article
Abstract: The enzyme β-hydroxydecanoyl thioester dehydrase, a requisite component of the fatty acid synthetase system of Escherichia coli, catalyzes the reversible interconversion of the thioesters of β-hydroxydecanoic acid, trans-α,β-decenoic acid, and cis-β, γ-decenoic acid. All activities of the dehydrase are strongly inhibited by 3-decynoyl-N-acetylcysteamine. A marked preference for C10 substrates has previously been noted. For further elucidation of dehydrase specificity, kinetic parameters for the enzymatic dehydration and isomerization were determined with a series of substrates varying in chain length from eight to 12 carbon atoms in the acyl moiety. Inhibition constants for β,γ-acetylenic thioesters of the same series were also measured. The data show a remarkable parallelism between the relative activities of substrates and inhibitors as a function of carbon chain length. The inhibitor 3-decynoyl-N-acetylcysteamine appears to be irreversibly bound to the dehydrase.
Source: Journal of Biological Chemistry
Authors: G M Helmkamp, R R Rando, D J H Brock, K Bloch
Institution: Harvard University
Language: English
Subfield: Biochemistry
Domain: Life Sciences
Open Access status: hybrid
Estimated APC paid: $3,430
OpenAlex ID: W2127434990