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Structures of apo and holo tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K(+) ions
Tyrosine phenol-lyase, a tetrameric pyridoxal-5′-phosphate dependent enzyme, catalyses the reversible hydrolytic cleavage of l-tyrosine to phenol and ammonium pyruvate. Here we describe the crystal structure of the Citrobacter freundii holoenzyme at 1.9 Å resolution. The structure reveals a network...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
2006
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2691550/ https://ncbi.nlm.nih.gov/pubmed/16768450 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi0601858 |
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