Search Results - "Faleev, N. G."

Kinetic and spectral parameters of interaction of Citrobacter freundii methionine γ-lyase with amino acids by Morozova, E. A., Bazhulina, N. P., Anufrieva, N. V., Mamaeva, D. V., Tkachev, Y. V., Streltsov, S. A., Timofeev, V. P., Faleev, N. G., Demidkina, T. V.

“…Kinetic parameters of Citrobacter freundii methionine γ-lyase were determined with substrates in γ-elimination reactions as well as the inhibition of the…”
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Spatial structure and the mechanism of tyrosine phenol-lyase and tryptophan indole-lyase by Demidkina, T. V, Antson, A. A, Faleev, N. G, Phillips, R. S, Zakomirdina, L. N

“…Bacterial tyrosine phenol-lyase [EC 4.1.99.2] and tryptophan indole-lyase [EC 4.1.99.1] are pyridoxal 5'-phosphate dependent β-eliminating lyases that catalyze…”
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L-methionine gamma-lyase from Citrobacter freundii: cloning of the gene and kinetic parameters of the enzyme by Manukhov, I V, Mamaeva, D V, Morozova, E A, Rastorguev, S M, Faleev, N G, Demidkina, T V, Zavilgelsky, G B

“…It is shown for the first time for the Enterobacteriaceae family that a gene encoding L-methionine gamma-lyase (MGL) is present in the genome of Citrobacter…”
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Citrobacter freundii Methionine γ-Lyase: The Role of Serine 339 in the Catalysis of γ- and β-Elimination Reactions by Anufrieva, N V, Morozova, E A, Revtovich, S V, Bazhulina, N P, Timofeev, V P, Tkachev, Ya V, Faleev, N G, Nikulin, A D, Demidkina, T V

“…Serine 339 of the active site of Citrobacter freundii methionine γ-lyase (MGL) is a conserved amino acid in most pyridoxal 5’-phosphate-dependent enzymes of…”
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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 by Demidkina, T.V., Faleev, N.G., Papisova, A.I., Bazhulina, N.P., Kulikova, V.V., Gollnick, P.D., Phillips, R.S.

“…In the X-ray structure of tyrosine phenol-lyase (TPL) Asp214 is located at H-bonding distance from the N1 atom of the cofactor. This residue has been replaced…”
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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 Substrate by Faleev, N G, Tsvetikova, M A, Gogoleva, O I, Kulikova, V V, Revtovich, S V, Kochetkov, K A

“…In the reaction between tryptophan indole-lyase (TIL) and a substrate containing a bad leaving group (L-serine), general acid catalysis is required for the…”
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Role of arginine 226 in the mechanism of tryptophan indole-lyase from Proteus vulgaris by Kulikova, V V, Zakomirdina, L N, Bazhulina, N P, Dementieva, I S, Faleev, N G, Gollnick, P D, Demidkina, T V

“…In the spatial structure of tryptophanase from Proteus vulgaris the guanidinium group of arginine 226 forms a salt bridge with the 3;-oxygen atom of the…”
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Tryptophan indole-lyase from Proteus vulgaris: kinetic and spectral properties by Zakomirdina, L N, Kulikova, V V, Gogoleva, O I, Dementieva, I S, Faleev, N G, Demidkina, T V

“…An efficient method for purification of recombinant tryptophanase from Proteus vulgaris was developed. Catalytic properties of the enzyme in reactions with…”
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Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate by Barbolina, M.V., Phillips, R.S., Gollnick, P.D., Faleev, N.G., Demidkina, T.V.

“…Asn185 is an invariant residue in all known sequences of TPL and of closely related tryptophanase and it may be aligned with the Asn194 in aspartate…”
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l-methionine-γ-lyase in Citrobacter intermedius cells: Stereochemical requirements with respect to the thiol structure by Faleev, N.G., Troitskaya, M.V., Paskonova, E.A., Saporovskaya, M.B., Belikov, V.M.

“…The specificity of l-methionine-γ-lyase with respect to the stereochemical structure of the thiol substrate in the γ-substitution reaction has been…”
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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 Tyrosines by Faleev, N. G., Spirina, S.N., Ivoilov, V. S., Demidkina, T. V., Phillips, R. S.

“…Apparently homogeneous tyrosine phenol-lyase (TPL) from Erwinia herbicola has been prepared by a new method. The pH-dependencies of the main kinetic parameters…”
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Biologically active organophosphorous analogues of methionine in reactions catalyzed by L-methionine gamma-lyase by Alferov, K V, Faleev, N G, Demidkina, T V, Khurs, E N, Morozova, E A, Khomutov, R M

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Tyrosine phenol-lyase from Citrobacter intermedius: factors controlling substrate specificity by FALEEV, N. G, RUVINOV, S. B, DEMIDKINA, T. V, MYAGKIKH, I. V, GOLOLOBOV, M. YU, BAKHMUTOV, V. I, BELIKOV, V. M

“…L-Amino acids are competitive inhibitors of tyrosine phenol-lyase from Citrobacter intermedius. For non-branched amino acids the correlation exists between…”
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Use of PVA-cryogel entrapped Citrobacter intermedius cells for continuous production of 3-fluoro-L-tyrosine by LOZINSKY, V. I, FALEEV, N. G, ZUBOV, A. L, RUVINOV, S. B, ANTONOVA, T. V, VAINERMAN, E. S, BELIKOV, V. M, ROGOZHIN, S. V

“…The cells of Citrobacter intermedius (containing L-tyrosine phenol lyase which catalyses the synthesis of 3-fluoro-L-tyrosine from o-fluorophenol, pyruvate and…”
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Tyrosine phenol-lyase: the role of the coenzyme-binding residue Ser-254 in catalysis by Papisova, A I, Bazhulina, N P, Faleev, N G, Demidkina, T V

“…(ProQuest: Abstract omitted; see image)[PUBLICATION ABSTRACT]…”
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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 Substrate by Faleev, N. G., Tsvetikova, M. A., Gogoleva, O. I., Kulikova, V. V., Revtovich, S. V., Kochetkov, K. A.

“…In the reaction between tryptophan indole-lyase (TIL) and a substrate containing a bad leaving group (L-serine), general acid catalysis is required for the…”
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Enzymes accompanying tyrosine phenol lyase and the problem of its substrate specificity by FALEEV, N. G, VIKHA, YU. K, MARTINKOVA, N. S, BELIKOV, V. M

“…The cells of Escherichia intermedia A-21, known as a producer of tyrosine phenol lyase, are shown to produce D-serine dehydratase, L-serine dehydratase, and…”
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Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola by Pletnev, S.V, Isupov, M.N, Dauter, Z, Wilson, K.S, Faleev, N.G, Harutyunyan, E.G, Demidkina, T.V

“…New method of purification of tyrosine phenol-lyase from Erwinia herbicola has been developed. The enzyme obtained is homogeneous and characterised by a…”
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Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents by Faleev, N G, Dementieva, I S, Zakomirdina, L N, Gogoleva, O I, Belikov, V M

“…In water-methanol and water-dimethylformamide (DMF) (1:1 v/v) solutions tryptophanase from E.coli retains its abilities to form a quinonoid complex with…”
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Kinetic and spectral parameters of interaction of Citrobacter freundii methionine [gamma]-lyase with amino acids by Morozova, E A, Bazhulina, N P, Anufrieva, N V, Mamaeva, D V, Tkachev, Y V, Streltsov, S A, Timofeev, V P, Faleev, N G, Demidkina, T V

“…Kinetic parameters of Citrobacter freundii methionine γ-lyase were determined with substrates in γ-elimination reactions as well as the inhibition of the…”
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