https://www.selleckchem.com/pr....oducts/sabutoclax.ht
Fluorescence resonance energy transfer between PLP and W99, the enzyme's only tryptophan residue, supports ligand-induced closure of the active site, which shields the PLP cofactor from the solvent and increases the basicity of D232. These results provide new insight into amino acid metabolism in F. nucleatum and highlight the multiple catalytic roles of D232 in a new member of the fold type II family of PLP-dependent enzymes.Central-to-axial chirality transfer via C-N single bond oxidation was first achieved as a versatile and conce
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