EC Number |
Protein Variants |
Reference |
---|
2.6.1.78 | A168G |
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type |
759965 |
2.6.1.78 | E108K |
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type |
759965 |
2.6.1.78 | K12G |
naturally occuring mutant, the incompetent PATs of Rhizobium meliloti (UniProt ID P58350) has a G instead of K12 and shows reduced PAT activity at prephenate concentrations up to 2.5 mM using a coupled assay method. The mutant shows reduced activity and altered kinetics compared to the wild-type |
759178 |
2.6.1.78 | K12G |
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type |
-, 759178 |
2.6.1.78 | K169S |
site-directed mutagenesis, inactive with aspartate and glutamate |
759965 |
2.6.1.78 | K169V |
site-directed mutagenesis, inactive with glutamate, altered substrate binding kinetics compared to wild-type |
759965 |
2.6.1.78 | K306A |
site-directed mutagenesis, structure comparison with wild-type, overview. The alanine substitution of Lys306 prevents Schiff base formation with the cofactor, inactive mutant |
759965 |
2.6.1.78 | more |
site-directed mutagenesis, modeling, and molecular dynamics simulations reveal that K/R/Q12 residue (numbering according to Thermus thermophilus 1beta AAT) is a signature of the PAT function of 1bta AAT. It is present in the N-terminal flexible loop only in PAT competent 1beta-AAT and has a possible role in stabilizing prephenate by interacting with its 4-hydroxy group |
759178 |
2.6.1.78 | R445G |
site-directed mutagenesis, inactive mutant |
759965 |
2.6.1.78 | T84V |
site-directed mutagenesis, altered substrate binding kinetics compared to wild-type |
759965 |