Evidence that the acyl-O-esters are intermediates in the catalysis. The mechanism of rabbit mammary fatty acid synthase |
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Authors: | A D McCarthy D G Hardie |
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Institution: | Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA |
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Abstract: | The sequence acetyl-CoA leads to acetyl-O-enzyme leads to acetyl-S-acyl carrier protein has for the first time been demonstrated directly with a multifunctional (mammalian) fatty acid synthase. This was achieved by blocking of the active-site thiols of rabbit mammary fatty acid synthase with iodoacetamide. The modified enzyme was incubated with 14C]acetyl-CoA to form acetyl-O-enzyme, and acetyl-CoA was removed rapidly by centrifuge desalting. We were then able to demonstrate transfer of the acetyl group from 14C]acetyl-O-enzyme to the pantetheine thiol in a fragment of rabbit mammary fatty acid synthase containing the phosphopantetheine group, and to E. coli acyl carrier protein. |
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Keywords: | Cytochrome c Superoxide dismutase Ionic strength Dielectric constant Lysine residues Electrostatic facilitation SOD superoxide dismutase BESOD bovine erythrocyte superoxide dismutase |
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