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Original scientific paper
https://doi.org/10.5562/cca1915

Crystal Structure of Citrobacter freundii Asp214Ala Tyrosine Phenollyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine

Dalibor Milić   ORCID icon orcid.org/0000-0001-5760-6677 ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia
Tatyana V. Demidkina ; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov Street, Moscow 119991, Russia
Lyudmila N. Zakomirdina ; Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 32 Vavilov Street, Moscow 119991, Russia
Dubravka Matković-Čalogović   ORCID icon orcid.org/0000-0003-4909-8312 ; Department of Chemistry, Faculty of Science, University of Zagreb, Horvatovac 102a, 10000 Zagreb, Croatia
Alfred A. Antson ; Structural Biology Laboratory, Department of Chemistry, University of York, Heslington, York YO10 5YW, United Kingdom

Fulltext: english, pdf (5 MB) pages 283-288 downloads: 899* cite
APA 6th Edition
Milić, D., Demidkina, T.V., Zakomirdina, L.N., Matković-Čalogović, D. & Antson, A.A. (2012). Crystal Structure of Citrobacter freundii Asp214Ala Tyrosine Phenollyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine. Croatica Chemica Acta, 85 (3), 283-288. https://doi.org/10.5562/cca1915
MLA 8th Edition
Milić, Dalibor, et al. "Crystal Structure of Citrobacter freundii Asp214Ala Tyrosine Phenollyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine." Croatica Chemica Acta, vol. 85, no. 3, 2012, pp. 283-288. https://doi.org/10.5562/cca1915. Accessed 21 Oct. 2021.
Chicago 17th Edition
Milić, Dalibor, Tatyana V. Demidkina, Lyudmila N. Zakomirdina, Dubravka Matković-Čalogović and Alfred A. Antson. "Crystal Structure of Citrobacter freundii Asp214Ala Tyrosine Phenollyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine." Croatica Chemica Acta 85, no. 3 (2012): 283-288. https://doi.org/10.5562/cca1915
Harvard
Milić, D., et al. (2012). 'Crystal Structure of Citrobacter freundii Asp214Ala Tyrosine Phenollyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine', Croatica Chemica Acta, 85(3), pp. 283-288. https://doi.org/10.5562/cca1915
Vancouver
Milić D, Demidkina TV, Zakomirdina LN, Matković-Čalogović D, Antson AA. Crystal Structure of Citrobacter freundii Asp214Ala Tyrosine Phenollyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine. Croatica Chemica Acta [Internet]. 2012 [cited 2021 October 21];85(3):283-288. https://doi.org/10.5562/cca1915
IEEE
D. Milić, T.V. Demidkina, L.N. Zakomirdina, D. Matković-Čalogović and A.A. Antson, "Crystal Structure of Citrobacter freundii Asp214Ala Tyrosine Phenollyase Reveals that Asp214 is Critical for Maintaining a Strain in the Internal Aldimine", Croatica Chemica Acta, vol.85, no. 3, pp. 283-288, 2012. [Online]. https://doi.org/10.5562/cca1915

Abstracts
Tyrosine phenol-lyase (TPL) is a pyridoxal-5′-phosphate (PLP) dependent enzyme which catalyzes β-elimination of L-tyrosine. In the holoenzyme the protonated pyridinium N1 atom of the PLP cofactor is hydrogen-bonded to the side chain of Asp214. Here we report the X-ray structure of C. freundii D214A TPL determined at 1.9 Å resolution. Comparison with the structure of the wild-type TPL shows that the D214A replacement induced significant conformational reorganization in the active site leading to its partial closure. Significantly, in D214A TPL the strain in the internal aldimine is completely released and the pyridine N1 atom of PLP is deprotonated. These observations explain the considerably reduced activity of the D214A TPL towards its substrates [T. V. Demidkina et al., Biochim. Biophys. Acta, Proteins Proteomics 1764 (2006) 1268–1276]. The reported structure reveals that Asp214 is critical for maintaining the strain in the internal aldimine. We argue that this strain is used by the enzyme to accelerate the transaldimination reaction, the first step in the enzymatic catalysis.(doi: 10.5562/cca1915)

Keywords
tyrosine phenol-lyase; chemical strain; internal aldimine; pyridoxal 5′-phosphate; X-ray structure

Hrčak ID: 92038

URI
https://hrcak.srce.hr/92038

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