Fig. 2: The enzyme–substrate-mimicking complex (Dat/Ac-CoA/tryptophol) and enzyme-product complex (Dat/CoA/Ac-TRYP) have similar structures. | Communications Biology

Fig. 2: The enzyme–substrate-mimicking complex (Dat/Ac-CoA/tryptophol) and enzyme-product complex (Dat/CoA/Ac-TRYP) have similar structures.

From: An essential role of acetyl coenzyme A in the catalytic cycle of insect arylalkylamine N-acetyltransferase

Fig. 2

a Superposition of Dat/Ac-CoA/tryptophol (gray, substrate-mimicking complex, PDB code: 6K80) and Dat/CoA/Ac-TRYP (orange, product complex, PDB code: 5GI9). The Cα-based RMSD of the two structures is 0.10 Å (183 atoms), and the all-atom-based RMSD is 0.65 Å (1688 atoms). Ac-CoA, tryptophol, CoA, and Ac-TRYP are shown as sticks. The solvent-accessible tunnel is shown in gray. b The aromatic residues of the substrate-binding pocket. The distances of Met121 to Tyr64 and Phe114 (green dashed line) were 5.5 and 7.0 Å, respectively. The distances from the center of the indole ring of the substrate to Phe43, Tyr64, and Phe114 (purple dashed line) were 5.0, 5.8, and 5.8 Å, respectively. c Cofactor-binding site and catalytic triad.

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