The purpose of this research was to develop new strains of Escherichia coli with improved fatty acid biosynthesis. ${eta}$-Ketoacyl acyl carrier protein synthase III (fabH) catalyzes the first step in the synthesis of fatty acids in parallel with acetyl-CoA carboxylase (accABC) and malonyl-CoA: acyl carrier protein transacylase (fabD) in Escherichia coli K-12 MG1655. The enzyme encoded by the fabH gene leads to an increase in the synthesis of short-chain-cength fatty acids and a strong preference for acetyl-CoA, as it produces only straight chain fatty acids (SCFAs). It also seems to play a role in determining the type and composition of fatty acids produced. In this study, metabolically engineered strains of E. coli K-12 MG1655 containing fabH or accA::accBC::fabD or accA::accBC::fabD::fabH gene-inserted expression vector (pTrc99A) were constructed. To observe the effects of overexpression, the production of malonic acid, a pathway intermediate, and fatty acids was analyzed. The resulting recombinant strains produced total lipids up to approximately 1.2 ~ 1.6 fold higher than that of wild-type E. coli. The production of hexadecanoic acid was especially enhanced up to approximately 4.8 fold in E. coli SGJS13 as compared to E. coli SGJS11.