Abstract
Biotin protein ligase (BPL) catalyses the synthesis of an activated form of biotin, biotinyl-5'-AMP, from substrates biotin and ATP followed by biotinylation of the biotin carboxyl carrier protein subunit of acetyl-CoA carboxylase. In order to visualize the structural feature of the BPL reaction, crystal structures of BPL from Pyrococcus horikoshii OT3 have been determined in an unliganded form and three liganded forms with biotin, ADP and the reaction intermediate biotinyl-5'-AMP. The exact locations of the ligands and the active site residues allow us to propose a general scheme for the first step of the reaction carried out by BPL.
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