Summary
Free amino acids are competitive inhibitors of tyrosine phenol lyase from Citrobacter intermedius The correlation exist between -RTlnKi. and side chain hydrophobicity. Aspartic and glutamic acids are anomalously strong inhibitors taking into consideration low hydrophobicity of their side chains. One can assume that the electrophilic group able to interact with the terminal C00−-group of aspartic and glutamic acids is located in the active site of the enzyme. The substrate specificity of tyrosine phenol-lyase is controlled during the stage of aromatic ring elimination. The OH-group in the p- position of the ring is the first necessary condition for the stage to proceed. The same stage is also sensitive to the steric parameters of the substituent in the ring which ensures the second factor of control.
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© 1987 Birkhäuser Verlag Basel
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Faleev, N.G. et al. (1987). The Substrate Specificity of Tyrosine Phenol-Lyase During the Different Stages of Enzymatic Process. In: Korpela, T.K., Christen, P. (eds) Biochemistry of Vitamin B6 . Birkhäuser Congress Reports. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-9308-4_39
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DOI: https://doi.org/10.1007/978-3-0348-9308-4_39
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