Summary
Tyrosine phenol-lyase is a tetramer composed of four identical subunits. The active form of the tyrosine phenol-lyase is the protonated form of the holoenzyme produced by monovalent cations. The enzyme catalyses a side transamination reaction. Crystals of the apoenzyme suitable for X-Ray analysis were obtained.
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References
Demidkina, T.V., Myagkikh, I.V., Faleev, N.G., and Belikov, V.M. (1984) Biokhimia 49, 32–37 (in Russian).
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© 1987 Birkhäuser Verlag Basel
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Demidkina, T.V., Myagkikh, I.V. (1987). Structural and Catalytic Properties of Citrobacter Intermedius Tyrosine Phenol-Lyase. 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_40
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DOI: https://doi.org/10.1007/978-3-0348-9308-4_40
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