Site-directed mutants of charged residues in the active site of tyrosine hydroxylase

A study was conducted to analyze charged residues in the hydrophobic cleft of the active site of tyrosine hydroxylase. The 380B DNA synthesizer from Applied Biosystems was utilized to prepare the oligonucleotides. Plasmids were then introduced into Escherichia coli or BL2(DE3) cells to promote bacteria cell growth. Experimental results indicated that glutamate 332 promotes tetrahydropterin binding.