Abstract: Disclosed herein is a low-cost method to maximize malonyl-CoA production in E. coli, and consequently a high yield of its derived bioproducts.

Abstract: An efficient synthesis for the selective and efficient 1′-N derivatization of biotin is reported. The derivatized biotin acts as a stable analog of the carboxyphosphate intermediate in naturally-occurring biotin-mediated CO2 transfer. The synthesis may readily be scaled up to perform large-scale, selective acylations of biotin. The stable analog of the intermediate can inhibit the activity of the biotin carboxylase enzymes such as acetyl CoA carboxylase, and HIV protease. The functionalization at the 1′-N of biotin results in the attachment of an electrophilic “handle” amenable to reaction with a wide variety of nucleophiles to generate a new family of biotin analogs.

Abstract: A method is disclosed for inhibiting carboxyltransferase with bisubstrate analogs. One such analog has been shown to inhibit the carboxyltransferase component of E. coli acetyl-CoA carboxylase. It is also expected to inhibit mammalian acetyl-CoA carboxylase, and thereby to act as an antiobesity agent and an anti-cancer agent.

Abstract: An efficient synthesis for the selective and efficient 1′-N derivatization of biotin is reported. The derivatized biotin acts as a stable analog of the carboxyphosphate intermediate in naturally-occurring biotin-mediated CO2 transfer. The synthesis may readily be scaled up to perform large-scale, selective acylations of biotin. The stable analog of the intermediate can inhibit the activity of the biotin carboxylase enzymes such as acetyl CoA carboxylase, and HIV protease. The functionalization at the 1′-N of biotin results in the attachment of an electrophilic “handle” amenable to reaction with a wide variety of nucleophiles to generate a new family of biotin analogs.

Abstract: An efficient synthesis for the selective and efficient 1′-N derivatization of biotin is reported. The derivatized biotin acts as a stable analog of the carboxyphosphate intermediate in naturally-occurring biotin-mediated CO2 transfer. The synthesis may readily be scaled up to perform large-scale, selective acylations of biotin. The stable analog of the intermediate can inhibit the activity of the biotin carboxylase enzymes such as acetyl CoA carboxylase, and HIV protease. The functionalization at the 1′-N of biotin results in the attachment of an electrophilic “handle” amenable to reaction with a wide variety of nucleophiles to generate a new family of biotin analogs.