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Acta Naturae|November 14, 2019
The Catalytic Mechanisms of the Reactions between Tryptophan Indole-Lyase and Nonstandard Substrates: The Role of the Ionic State of the Catalytic Group Accepting the Cα Proton of the SubstrateN G Faleev, M A Tsvetikova, O I Gogoleva, et al.
Molekuliarnaia Biologiia|May 1, 1991
[Factors, determining the effectiveness of tryptophanase interaction with amino acids]N G Faleev, S B Ruvinov, L N Zakomyrdina, et al.
European Journal of Biochemistry|November 1, 1988
Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificityN G Faleev, S B Ruvinov, T V Demidkina, et al.
Biochemistry and Molecular Biology International|February 1, 1996
Purification and crystals of tyrosine phenol-lyase from Erwinia herbicolaS V Pletnev, M N Isupov, Z Dauter, et al.
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|April 18, 2006
L-methionine gamma-lyase from Citrobacter freundii: cloning of the gene and kinetic parameters of the enzymeI V Manukhov, D V Mamaeva, E A Morozova, et al.
Biochemistry. Biokhimiia|December 4, 2003
Role of arginine 226 in the mechanism of tryptophan indole-lyase from Proteus vulgarisV V Kulikova, L N Zakomirdina, N P Bazhulina, 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.
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