MD and QM/MM study on catalytic mechanism of a FAD-dependent enzyme ORF36: For nitro sugar biosynthesis
A phenylalanine/leucine residue pair is important for FAD binding. Three elementary catalytic steps were found. Hydroxylation step is the rate-determining step. Oxygen atom that comes from the coenzyme FADHOOH stays in the product. Of all the residues, Ser162 suppresses the hydroxylation reaction most.
hydroxylation everninomicin molecular dynamics mechanical/molecular mechanical method electrostatic influence