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Results 1 - 7 of 7
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.14.13.243Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.243A106E 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
Show all pathways known for 1.14.13.243Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.243A113H mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole -, 749719
Show all pathways known for 1.14.13.243Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.243A113I mutation in subunit TomA3. Mutant enzyme produces primarily indirubin from indole -, 749719
Show all pathways known for 1.14.13.243Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.243A113V mutation in subunit TomA3, colony turns blue. Mutant enzyme produces primarily indigo from indole -, 749719
Show all pathways known for 1.14.13.243Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.243V106A 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
Show all pathways known for 1.14.13.243Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.243V106A/A113G mutation in subunit TomA3. Mutant enzyme produces primarily isatin from indole -, 749719
Show all pathways known for 1.14.13.243Display the word mapDisplay the reaction diagram Show all sequences 1.14.13.243V106M 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
Results 1 - 7 of 7