Fig. 5: Crystallographic and spectroscopic characterization of H275E.
From: Substrate multiplexed protein engineering facilitates promiscuous biocatalytic synthesis
a Internal aldimine structure of H275E (light blue, PDB: 7RNQ) is superimposed with the corresponding structure of 2B9 (gray, PDB: 6AM7). b Addition of 20 mM l-serine (Ser) to 2B9 (gray), results in two peaks corresponding to external aldimine E(Aex1) and amino acrylate, E(A-A), intermediates. Addition of 20 mM Ser to H275E (pink) shows a dominant peak corresponding to E(A-A). A representative enzyme-only trace is shown in black. Spectra were collected at 37 °C. c X-ray structures of H275E. i. Trp binding is shown in magenta from PDB: 7ROF. ii. 4-Cl-Trp binding is shown in cyan from PDB: 7RNP. Hydrogen and halogen bonds are shown in orange and purple dashes, respectively.
