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Site-directed mutagenesis of His343-->Ala in Citrobacter freundii tyrosine phenol-lyase. Effects on the kinetic mechanism and rate-determining step.
Chen H, Gollnick P, Phillips RS. Chen H, et al. Among authors: gollnick p. Eur J Biochem. 1995 Apr 15;229(2):540-9. Eur J Biochem. 1995. PMID: 7744078 Free article.
His343 in Citrobacter freundii tyrosine phenol-lyase is conserved in all known sequences of both tyrosine phenol-lyase and tryptophan indole-lyase; it is located near the active-site Lys257 in C. freundii tyrosine phenol-lyase [Antson, A. A., Demidkina, T. V., Gollnick, …
His343 in Citrobacter freundii tyrosine phenol-lyase is conserved in all known sequences of both tyrosine phenol-lyase and tryptophan indole …
Three-dimensional structure of tyrosine phenol-lyase.
Antson AA, Demidkina TV, Gollnick P, Dauter Z, von Tersch RL, Long J, Berezhnoy SN, Phillips RS, Harutyunyan EH, Wilson KS. Antson AA, et al. Among authors: gollnick p. Biochemistry. 1993 Apr 27;32(16):4195-206. doi: 10.1021/bi00067a006. Biochemistry. 1993. PMID: 7916622
The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.
Sundararaju B, Antson AA, Phillips RS, Demidkina TV, Barbolina MV, Gollnick P, Dodson GG, Wilson KS. Sundararaju B, et al. Among authors: gollnick p. Biochemistry. 1997 May 27;36(21):6502-10. doi: 10.1021/bi962917+. Biochemistry. 1997. PMID: 9174368
Aspartic acid 214 in Citrobacter freundii tyrosine phenol-lyase ensures sufficient C--H-acidity of the external aldimine intermediate and proper orientation of the cofactor at the active site.
Demidkina TV, Faleev NG, Papisova AI, Bazhulina NP, Kulikova VV, Gollnick PD, Phillips RS. Demidkina TV, et al. Among authors: gollnick pd. Biochim Biophys Acta. 2006 Jul;1764(7):1268-76. doi: 10.1016/j.bbapap.2006.05.001. Epub 2006 May 16. Biochim Biophys Acta. 2006. PMID: 16793353
200 results