Abstract
This work was aimed at studying the effect of monovalent inorganic cations (Li +, Na +, K +, Rb +, Cs +, NH 4 +) on the catalytic and spectral characteristics of tyrosine phenol-lyase from Citrobacter intermedius. These cations were shown to influence the proportion of the ß-elimination reaction rate to the rate of side transamination reaction. Most of the monovalent cations are non-competitive activators of the ß-elimination reaction; Li + exerts no effect on the enzyme activity in this reaction; Na + is an inhibitor of the ß-elimination reaction. The activation of tyrosine phenol-lyase by monovalent cations stems from the creation of an active holoenzyme form (λ max420 nm) due to conformational rearrangements of the protein molecule.
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