Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli

• DOI: 10.1042/bj2500789
• Publication Date: 2015-08-10T21:10:03Z
• Authors: P N Lowe; S Rhodes
• Keywords: Iodoacetamide; Acetyltransferases; Acyl carrier protein

A multi-step procedure has been developed for the purification of [acyl-carrier-protein] acetyltransferase from Escherichia coli, which allows production small amounts homogeneous enzyme. The subunit Mr was estimated to be 29,000 and native 61,000, suggesting a homodimeric structure. catalytic properties enzyme are consistent with Bi Ping Pong mechanism existence an acetyl-enzyme intermediate in cycle. inhibited by N-ethylmaleimide more slowly iodoacetamide reactions protected substrate, acetyl-CoA. However, apparently only weakly thiol-specific reagent methyl methanethiosulphonate. nature is discussed relationship that found other similar enzymes E. yeast vertebrates.