1.13.11.8	A18W	site-directed mutagenesis, mutation in the betaa-subunit, residue Ala18b is located opening of the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme	741768	
1.13.11.8	F103H	site-directed mutagenesis, mutation in the alpha-subunit, residue Phe103a is located in the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme	741768	
1.13.11.8	F103L	site-directed mutagenesis, mutation in the alpha-subunit, residue Phe103a is located in the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme	741768	
1.13.11.8	F103T	site-directed mutagenesis, mutation in the alpha-subunit, residue Phe103a is located in the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme	741768	
1.13.11.8	F103T	site-directed mutagenesis, mutation in the alpha-subunit, the mutant shows enhanced utilization of substrates gallate and 3-O-methylgallate, but not of protocatechuate, compared to the wild-type enzyme	743708	
1.13.11.8	F103V	site-directed mutagenesis, mutation in the alpha-subunit, residue Phe103a is located in the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme	741768	
1.13.11.8	F103V	site-directed mutagenesis, mutation in the alpha-subunit, the mutant shows enhanced utilization of substrates gallate and 3-O-methylgallate, but not of protocatechuate, compared to the wild-type enzyme	743708	
1.13.11.8	additional information	in silico docking of substrates to the enzyme mutants, and impact of Phe103alpha mutations on allosteric activation of alternate substrate dioxygenation, overview	743708