Fig. 5
From: A multi-enzyme cascade for efficient production of d-p-hydroxyphenylglycine from l-tyrosine
Improvement of the catalytic activity of CgDAPDHBC621 toward HPGA by “conformational rotation” strategy. a Directed evolution of the parent CgDAPDHBC621 for reductive amination of HPGA. b The binding pocket surface of CgDAPDHBC621. D-HPG is shown in purple. c The binding pocket surface of CgDAPDHBC621/D120S/W144S/I169P. D-HPG is shown in orange. d Docking of the D-HPG into the active site of CgDAPDHBC621/D120S/W144S/I169P. D-HPG is shown in orange, NADP+ cofactor is shown in cyan, residue S120 is shown in purple, L150 is shown in magenta, G151 is shown in yellow, and H152 is shown in green. The hydrogen bond between D-HPG and residues S120, L150, G151, and N270 are shown in green dash lines, respectively. The yellow dash lines denote d(C6HDAP−C4NNADP) and d(C6DAP−ND1His152), respectively. e Superposition of the D-HPG conformation in parent CgDAPDHBC621 and variant CgDAPDHBC621/D120S/W144S/I169P. f–g RMSD values calculated from MD simulations of CgDAPDHBC621 and CgDAPDHBC621/D120S/W144S/I169P. The highlight represented the changes of the region with noticeable movements for CgDAPDHBC621