N G Faleev - JoVE Visualize

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Biokhimiia (Moscow, Russia)|January 1, 1984

[Isolation and properties of tyrosine phenol-lyase from Citrobacter intermedius]T V Demidkina, I V Miagkikh, N G Faleev, et al.

Zeitschrift Fur Naturforschung. C, Journal of Biosciences|May 1, 1996

The catalytic mechanism of tyrosine phenol-lyase from Erwinia herbicola: the effect of substrate structure on pH-dependence of kinetic parameters in the reactions with ring-substituted tyrosinesN G Faleev, S N Spirina, V S Ivoilov, et al.

Molekuliarnaia Biologiia|November 1, 1987

[Substrate specificity of tyrosine-phenol-lyase. Electron and steric control at the stage of aromatic moiety elimination]N G Faleev, S B Ruvinov, V I Bakhmutov, et al.

Biochemistry and Molecular Biology International|April 1, 1995

2-Methyl-L-tryptophan is a substrate of tryptophanaseN G Faleev, O I Gogoleva, I S Dementieva, et al.

Protein Engineering|April 25, 2000

Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediateM V Barbolina, R S Phillips, P D Gollnick, et al.

Molekuliarnaia Biologiia|January 1, 1988

[Interaction of tyrosine-phenol-lyase from Citrobacter intermedius with amino acids and their derivatives: factors determining the effectiveness of binding]N G Faleev, S B Ruvinov, T V Demidkina, et al.

Biochemistry and Molecular Biology International|August 1, 1994

Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solventsN G Faleev, I S Dementieva, L N Zakomirdina, et al.

Molekuliarnaia Biologiia|May 12, 2009

[Spatial structure and mechanism of tyrosine phenol-lyase and tryptophan indole-lyase]T V Demidkina, A A Anston, N G Faleev, et al.

Biochemistry. Biokhimiia|December 4, 2002

Tryptophan indole-lyase from Proteus vulgaris: kinetic and spectral propertiesL N Zakomirdina, V V Kulikova, O I Gogoleva, et al.

Bioorganicheskaia Khimiia|August 1, 1990

[Catalytic properties of E. coli tryptophanase in a 50% aqueous solution of methanol and dimethylformamide]N G Faleev, M B Saporovskaia, V M Belikov, et al.

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Showing results (1-10 of 20) with videos related to

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Biokhimiia (Moscow, Russia)|January 1, 1984

[Isolation and properties of tyrosine phenol-lyase from Citrobacter intermedius]T V Demidkina, I V Miagkikh, N G Faleev, et al.

Zeitschrift Fur Naturforschung. C, Journal of Biosciences|May 1, 1996

The catalytic mechanism of tyrosine phenol-lyase from Erwinia herbicola: the effect of substrate structure on pH-dependence of kinetic parameters in the reactions with ring-substituted tyrosinesN G Faleev, S N Spirina, V S Ivoilov, et al.

Molekuliarnaia Biologiia|November 1, 1987

[Substrate specificity of tyrosine-phenol-lyase. Electron and steric control at the stage of aromatic moiety elimination]N G Faleev, S B Ruvinov, V I Bakhmutov, et al.

Biochemistry and Molecular Biology International|April 1, 1995

2-Methyl-L-tryptophan is a substrate of tryptophanaseN G Faleev, O I Gogoleva, I S Dementieva, et al.

Protein Engineering|April 25, 2000

Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediateM V Barbolina, R S Phillips, P D Gollnick, et al.

Molekuliarnaia Biologiia|January 1, 1988

[Interaction of tyrosine-phenol-lyase from Citrobacter intermedius with amino acids and their derivatives: factors determining the effectiveness of binding]N G Faleev, S B Ruvinov, T V Demidkina, et al.

Biochemistry and Molecular Biology International|August 1, 1994

Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solventsN G Faleev, I S Dementieva, L N Zakomirdina, et al.

Molekuliarnaia Biologiia|May 12, 2009

[Spatial structure and mechanism of tyrosine phenol-lyase and tryptophan indole-lyase]T V Demidkina, A A Anston, N G Faleev, et al.

Biochemistry. Biokhimiia|December 4, 2002

Tryptophan indole-lyase from Proteus vulgaris: kinetic and spectral propertiesL N Zakomirdina, V V Kulikova, O I Gogoleva, et al.

Bioorganicheskaia Khimiia|August 1, 1990

[Catalytic properties of E. coli tryptophanase in a 50% aqueous solution of methanol and dimethylformamide]N G Faleev, M B Saporovskaia, V M Belikov, et al.

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