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  • Title: New design platform for malonyl-CoA-acyl carrier protein transacylase.
    Author: Hong SK, Kim KH, Park JK, Jeong KW, Kim Y, Kim EE.
    Journal: FEBS Lett; 2010 Mar 19; 584(6):1240-4. PubMed ID: 20176020.
    Abstract:
    Malonyl-CoA-acyl carrier protein transacylase (MCAT) transfers the malonyl group from malonyl-CoA to holo-acyl carrier protein (ACP), and since malonyl-ACP is a key building block for fatty-acid biosynthesis it is considered as a promising antibacterial target. The crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae have been determined at 1.46 and 2.1A resolution, respectively. In the SaMCAT structure, the N-terminal expression peptide of a neighboring molecule running in the opposite direction of malonyl-CoA makes extensive interactions with the highly conserved "Gly-Gln-Gly-Ser-Gln" stretch, suggesting a new design platform. Mutagenesis results suggest that Ser91 and His199 are the catalytic dyad.
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