2.3.1.39	malfunction	functional replacement of the fabD gene with amber mutation of Escherichia coli temperature-sensitive LA2-89 strain by Eimeria tenella EtMCAT demonstrates that EcFabD and EtMCAT perform the same biochemical function	
2.3.1.39	malfunction	the effect of overexpressing four different malonyl transacylases on fatty acid production is evaluated in an Escherichia coli fatty acid overproducing strain ML103(pXZ18). The strain carrying an acyl-ACP TE gene and a fabD gene from Escherichia coli, Streptomyces avermitilis MA-4680, or Streptomyces coelicolor A3 produce more free fatty acid than the control strain, whereas the strain carrying an acyl-ACP TE gene and a fabD gene from Clostridium acetobutylicum ATCC 824 produce similar quantity of free fatty acid as the control strain	
2.3.1.39	malfunction	disease variants of the enzyme lead to a structurally unstable protein with significantly reduced intracellular expression	
2.3.1.39	malfunction	enzyme mutants exhibit an embryo-lethal phenotype because of the arrest of embryo development at the globular stage	
2.3.1.39	metabolism	key enzyme in fatty acid biosynthesis	
2.3.1.39	metabolism	malonyl CoA-acyl carrier protein transacylase is closely associated with the FASII pathway of fatty acid biosynthesis	
2.3.1.39	metabolism	enzyme overexpression can weaken tricarboxylic acid, accelerate glucose absorption by improving membrane fluidity and permeability, and enhance carbon flux to the polyunsaturated fatty acid synthesis. Lipid and polyunsaturated fatty acid concentrations are increased by 10.1 and 24.5% with enzyme overexpression, respectively. Docosahexaenoic acid and eicosapentaenoic acid yield are enhanced 81.5 and 172.5%, respectively	
2.3.1.39	metabolism	lipid and polyunsaturated fatty acid concentration are increased by 10.1 and 24.5% with malonyl-CoA: ACP transacylase overexpression, respectively. The intracellular tricarboxylic acid cycle is weakened and glucose absorption is accelerated in the engineered strain. In the mevalonate pathway, intracellular carotene content is decreased, and the carbon flux is redirected toward synthesis of polyunsaturated fatty acid	
2.3.1.39	metabolism	the enzyme is an essential enzyme of the fatty acid synthesis II pathway. It performs initiation reaction to form malonyl-ACP, which is a key building block in fatty acid biosynthesis. Aporphine alkaloids can act as antibacterial agents and possible target of these compounds could be the FabD enzyme	
2.3.1.39	additional information	residues Arg113, Ser88 and His188 constitute cthe enzyme's atalytic triad. Structure homology modeling by molecular replacement using the enzyme from Escherichia coli, PDB: 1MLA, as a search model	
2.3.1.39	physiological function	enzyme overexpressing Nannochloropsis oceanica shows a higher growth rate and photosynthetic efficiency. Enzyme overexpression significantly alters the fatty acid composition. The levels of myristic acid, palmitic acid and palmitoleic acid tended to increase. The composition of eicosapentaenoic acid increases by 8% in transformed lines compared with wild type	
2.3.1.39	physiological function	the enzyme essential for cell division and its overexpression increases storage oil content	
2.3.1.39	physiological function	the enzyme plays an essential role in mitochondrial function and maintenance of retinal ganglion cell axons	
2.3.1.39	physiological function	the key enzyme of mitochondrial fatty acid synthesis contributes to insulin resistance