Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

PubChem13968 (2S)-2-amino-3-(3-fluoro-4- hydroxy...

Synonyms: SureCN274651, AG-G-94987, AG-G-95155, AG-L-63755, CHEBI:46534, ...

Faleev, N.G. et al., Barbolina, M.V. et al., Phillips, R.S. et al.

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High impact information on ZINC00119457

Multiple kinetic isotope effect studies on the reactions of N185A TPL with suitable substrates, L-tyrosine and 3-fluoro-L-tyrosine, show that the principal mechanism of catalysis, suggested previously for the wild-type enzyme, does not change [1].
The reactions of 2-fluoro- and 3-fluoro-L-tyrosine with mushroom tyrosinase have been investigated [2].
When all the requirements of substrate specificity are fulfilled (L-tyrosine, 3-fluoro-L-tyrosine), the 'key' phenol-elimination step is not the rate-limiting one, the reaction velocity being determined by the preceding alpha-proton abstraction [3].

References

Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate. Barbolina, M.V., Phillips, R.S., Gollnick, P.D., Faleev, N.G., Demidkina, T.V. Protein Eng. (2000) [Pubmed]
Oxygenation of fluorinated tyrosines by mushroom tyrosinase releases fluoride ion. Phillips, R.S., Fletcher, J.G., Von Tersch, R.L., Kirk, K.L. Arch. Biochem. Biophys. (1990) [Pubmed]
Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificity. Faleev, N.G., Ruvinov, S.B., Demidkina, T.V., Myagkikh, I.V., Gololobov MYu, n.u.l.l., Bakhmutov, V.I., Belikov, V.M. Eur. J. Biochem. (1988) [Pubmed]

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