Fig. 5: Structures and catalytic mechanisms of KnmB1 and KnmB2.
From: Discovery and biosynthesis of karnamicins as angiotensin converting enzyme inhibitors
a Comparison of the overall structures of KnmB1 (green), KnmB2 (cyan), and p-hydroxybenzoate hydroxylase (PHBH; pdb:1pbe; pink). b Molecular docking of 27 in KnmB1. c Molecular docking of 24 in KnmB2. N, O, and S atoms are colored blue, red and yellow, respectively. C atoms in KnmB1 residues, KnmB2 residues, and small molecules are colored as green, cyan, and white, respectively. d Proposed catalytic mechanism of KnmB1. e Proposed catalytic mechanism of KnmB2. R is ribityl adenosine diphosphate for FAD.
