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Biochimica Et Biophysica Acta|June 24, 2006
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 siteT V Demidkina, N G Faleev, A I Papisova, et al.Biochemistry. Biokhimiia|June 7, 2011
Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine γ-lyase with substratesS V Revtovich, E A Morozova, E N Khurs, et al.Molekuliarnaia Biologiia|April 8, 2015
[NMR screening of potential inhibitors of Citrobacter freundii methionine]E A Batuev, A Iu Lizunov, E A Morozova, et al.Biochemistry|May 27, 1997
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 specificityB Sundararaju, A A Antson, R S Phillips, et al.Biomedicine & Pharmacotherapy = Biomedecine & Pharmacotherapie|February 9, 2017
Plasma methionine depletion and pharmacokinetic properties in mice of methionine γ-lyase from Citrobacter freundii, Clostridium tetani and Clostridium sporogenesE A Morozova, N V Anufrieva, D Zh Davydov, et al.European Journal of Biochemistry|November 18, 2000
Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acidsN G Faleev, Y N Zhukov, E N Khurs, et al.Biochemistry. Biokhimiia|December 21, 2010
Kinetic and spectral parameters of interaction of Citrobacter freundii methionine γ-lyase with amino acidsE A Morozova, N P Bazhulina, N V Anufrieva, et al.Acta Naturae|August 4, 2022
Citrobacter freundii Methionine γ-Lyase: The Role of Serine 339 in the Catalysis of γ- and β-Elimination ReactionsN V Anufrieva, E A Morozova, S V Revtovich, et al.FEBS Letters|May 18, 1992
The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5'-phosphate-dependent enzymeA A Antson, B V Strokopytov, G N Murshudov, et al.Biochemistry|April 27, 1993
Three-dimensional structure of tyrosine phenol-lyaseA A Antson, T V Demidkina, P Gollnick, et al.Pageof 4