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Figure 1 | BMC Bioinformatics

Figure 1

From: Genome scale prediction of substrate specificity for acyl adenylate superfamily of enzymes based on active site residue profiles

Figure 1

Schematic representation of the acyl-adenylate superfamily and its various subfamilies. The figure shows the chemical structure of the substrates and products for the reactions catalyzed by members of each subfamily. The various subfamilies utilize different carboxylic acid substrates and transfer acyl moiety to either CoA or enzyme bound phosphopantetheine arm. The luciferase catalyzes conversion of luciferin to oxyluciferin. All the subfamilies are known to take up a similar 3-dimensional fold (depicted in centre) which has a large N-terminal domain and a small C-terminal domain. The structure shown is the adenylation domain of gramicidin synthetase (PDB code: 1AMU). The cofactor AMP (orange) and substrate Phenylalanine (red), shown in CPK, bind in the cleft separating the two domains. The substrate binding residues are shown in cyan as ball and stick.

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