In silico characterization of acetyl-CoA carboxylase from Staphylococcus aureus and Escherichia coli: A comparative...

Acetyl-CoA carboxylase (ACCase) catalyses the carboxylation of acetyl-CoA to malonyl-CoA and is vital for producing polyketides from acetyl-CoA. The enzyme is highly conserved for bacteria and may serve as the target for generating new antibacterial drugs. Therefore, characterizing the sequence and structure of these enzymes is very important. A comparative in silico study was done using Staphylococcus aureus and Escherichia coli to understand the stability and functionality of the enzyme from both Gram-positive and Gram-negative bacteria. It was found that S. aureus has predominantly charged and polar uncharged residues in its hydrophobic regions. The higher polarity and high hydrophilicity of S. aureus also raise its thermal stability and pathogenicity. The abundance of charged residues strengthens the protein through helix stabilizations in S. aureus. The large size of the ligand-binding pocket also makes it a promising drug target for S. aureus. S. aureus was found to increase the number of intra-protein interactions significantly. Finally, the molecular dynamics simulation (MDS) showed that ACCase from S. aureus is more stable and more compact.