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New design platform for malonyl‐CoA‐acyl carrier protein transacylase
Author(s) -
Hong Seung Kon,
Kim Kook Han,
Park Joon Kyu,
Jeong Ki-Woong,
Kim Yangmee,
Kim Eunice EunKyeong
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.02.038
Subject(s) - acyl carrier protein , chemistry , biochemistry , mutagenesis , malonyl coa , stereochemistry , biosynthesis , fatty acid , enzyme , beta oxidation , mutation , gene
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 2.1 Å 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.