In recent years, the Center for Disease Control (CDC) has highlighted many bacteria as being either serious or urgent threats in terms of antibiotic resistance such as Salmonella enterica, Klebsiella, and Shigella. These bacteria are all members of the bacterial family Enterobacteriaceae, and therefore all produce a complex oligosaccharide known as the Enterobacterial Common Antigen (ECA). Consisting of a polymerized trisaccharide repeat, the ECA can be presented either on the outer membrane of the bacteria, or within the periplasmic space. Although discovered in 1963, the exact function of the ECA has remained unknown. Some research points to involvement in virulence of Salmonella, and more recently, the regulation of membrane permeability. The two enzymes involved in the biosynthesis pathway that are focused on in this work include the acetyltransferase WecD and the ECA polymerase WzyE. High performance liquid chromatography (HPLC) was utilized to detect the production of the WecD reaction product, dTDP-Fuc4NAc. After using mass to confirm the product, colorimetric kinetics assays were performed using a 96-well plate and a spectrophotometer and using HPLC. When UDP-Fuc4NH2 was used as a substrate, turnover was significantly different from that of the dTDP-Fuc4NH2 reaction at the 30- and 60-minute time points, whereas they were similar at the 120-minute point. We also tested the difference between three constructs of WecD, and found that for most concentrations of substrate, there a significant difference in the rate of reactions at some concentration of AcCoA, however no clear pattern could be determined. When WzyE was incubated with ECA Lipid III for 60 minutes and analyzed via LCMS, a change in ECA Lipid III levels was observed that differed from that of the control reaction. This suggests that WzyE potentially worked in vitro but will require future studies to confirm.