1.14.13.243	A106E	mutation in hydroxylase alpha-subunit TomA3, variant degrades its natural substrate toluene 63% faster than wild-type, with 50% 2-methylphenol, 25% 3-methylphenol, and 25% 4-methylphenol being formed. Whole cells expressing the A106E variant have two times better naphthalene-to-1-naphthol activity than the wild-type, and the regiospecificity of the A106E variant is unchanged, with 98% 1-naphthol formed	-, 749647	
1.14.13.243	A113H	mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole	-, 749719	
1.14.13.243	A113I	mutation in subunit TomA3. Mutant enzyme produces primarily indirubin from indole	-, 749719	
1.14.13.243	A113V	mutation in subunit TomA3, colony turns blue. Mutant enzyme produces primarily indigo from indole	-, 749719	
1.14.13.243	V106A	mutation in subunit TomA3, colony turns green. Mutant degrades trichloroethylene, 1,1-dichloroethylene, and trans-dichloroethylene more rapidly than wild-type. Whole cells expressing the mutant synthesize 1-naphthol six times faster than wild-type enzyme	-, 750943	
1.14.13.243	V106A/A113G	mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole	-, 749719	
1.14.13.243	V106M	mutation of the alpha-hydroxylase subunit TomA3, improves both rate and enantioselectivity. Mutant oxidizes methyl phenyl sulfide to the corresponding sulfoxide at a rate of 3.0 nmol/min/mg protein compared with 1.6 for the wild-type enzyme, and the enantiomeric excess (pro-S) increases from 51% for the wild type to 88% for the mutant	-, 749648