Acetyl-coA carboxylase (ACC) is a central metabolic enzyme that catalyzes the committed step in fatty acid biosynthesis: biotin-dependent conversion of acetyl-coA to malonyl-coA. The bacterial carboxyltransferase (CT) subunit of ACC is a target for the design of novel therapeutics that combat severe, hospital-acquired infections resistant to the established classes of frontline antimicrobials. Here, we present the structures of the bacterial CT subunits from two prevalent nosocomial pathogens, Staphylococcus aureus and Escherichia coli, at a resolution of 2.0 and 3.0 A, respectively. Both structures reveal a small, independent zinc-binding domain that lacks a complement in the primary sequence or structure of the eukaryotic homologue.

The use of enzymes such as horseradish peroxidase (HRP) for degrading or removing toxic organics from synthetic wastewater has been demonstrated previously. Potential alternatives to HRP are other peroxidases, various ligninases, haloperoxidases and laccases. Results of this study indicate that a fungal peroxidase from Coprinus macrorhizus (CMP) has the capability to catalyze the same reactions as HRP. Similarly, in batch reactors the trend and removal efficiency of aromatic compounds by CMP from synthetic wastewater depend on the nature of the compound.

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