1 limination step, as we found previously with tyrosine phenol-lyase.

2                                Inhibition of tyrosine phenol-lyase, a bacterial enzyme responsible fo

3 umulated in the reaction of crystals of Y71F tyrosine phenol-lyase, an inactive mutant, with 3-F-l-Ty

4 of ring fluorinated analogs of tyrosine with tyrosine phenol-lyase and tryptophan indole-lyase (trypt

5  the reactions of fluorinated tyrosines with tyrosine phenol-lyase and tryptophan indole-lyase are du

6 mediate formation in the reactions with both tyrosine phenol-lyase and tryptophan indole-lyase.

7                                    Wild-type tyrosine phenol-lyase crystals bind l-Met and l-Phe to f

8 ophan indole-lyase and by wild type and Y71F tyrosine phenol-lyase crystals demonstrates that they ar

9 monia is catalyzed by the inducible enzyme L-tyrosine phenol lyase (EC 4.1.99.2).

10     The reaction of 3-fluoro-L-tyrosine with tyrosine phenol-lyase resulted in a peak at 500 nm with

11              The reaction of L-tyrosine with tyrosine phenol-lyase resulted in rapid formation of a s

12                       The X-ray structure of tyrosine phenol-lyase (TPL) complexed with a substrate a

13 ions of 2-azatyrosine and 3-azatyrosine with tyrosine phenol-lyase (TPL) from Citrobacter freundii ha

14                                              Tyrosine phenol-lyase (TPL) from Citrobacter freundii is

15                                              Tyrosine phenol-lyase (TPL) from Citrobacter freundii is

16                                              Tyrosine phenol-lyase (TPL) from Citrobacter freundii is

17 d to wild type and Y71F Citrobacter freundii tyrosine phenol-lyase was investigated in the crystallin