Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Marina A. Tsvetikova"'
Autor:
Maxim S. Oshchepkov, Leonid V. Kovalenko, Antonida V. Kalistratova, Inna N. Solovieva, Marina A. Tsvetikova, Olga N. Gorunova, Nataliya A. Bystrova, Konstantin A. Kochetkov
Publikováno v:
Agronomy, Vol 13, Iss 3, p 778 (2023)
Ureas, carbamates and oxamates are rather common structural motifs. They are present in both natural and synthetic compounds that exhibit a wide spectrum of biological activity. These derivatives of carbonic and oxalic acids are regularly employed as
Externí odkaz:
https://doaj.org/article/7ab0a02504a241488617d68c05b50a86
Autor:
Aleksandra A. Kuznetsova, Nicolai G. Faleev, Elena A. Morozova, Natalya V. Anufrieva, Olga I. Gogoleva, Marina A. Tsvetikova, Olga S. Fedorova, Tatyana V. Demidkina, Nikita A. Kuznetsov
Publikováno v:
Biochimie. 201:157-167
Methionine γ-lyase (MGL) is a pyridoxal 5'-phosphate-dependent enzyme catalyzing γ-elimination in l-methionine. Pyridoxal 5'-phosphate-dependent enzymes have unique spectral properties that allow to monitor sequential formation and decomposition of
Autor:
Vyacheslav S. Yufryakov, Viktoria V. Kulikova, Konstantin A. Kochetkov, N. G. Faleev, Natalya G. Kolotyrkina, Mikhail M. Ilyin, Tatiana V. Demidkina, Marina A. Tsvetikova
Publikováno v:
Mendeleev Communications. 31:236-238
Using a diastereomeric mixture of (S)-methionine S-oxide as an example, kinetic preference of methionine-γ-lyase toward a stereogenic center at the γ-sulfur atom of the (2S, RS) diastereomer was discovered for the first time.
Autor:
Vitalia V. Kulikova, Konstantin A. Kochetkov, Marina A. Tsvetikova, N. G. Faleev, S.V. Revtovich, Olga I. Gogoleva
Publikováno v:
Acta Naturae
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 group's elimination. During this stage, the proton originally bound to the C atom of the subst
Autor:
Nataliya A. Bystrova, Marina A. Tsvetikova, L. V. Kovalenko, A. V. Kalistratova, Konstantin A. Kochetkov, Maria S. Ivanova, Мaxim S. Oshchepkov
Publikováno v:
Journal of Agricultural Science. 13:36
Extreme environmental conditions increase the risk of abiotic stresses in plants, which reduce productivity of land. The investigation and developmentof synthetic approach to new antistress compounds, increasing the resistance of plants to negative f
Autor:
Nicolai G. Faleev, Robert S. Phillips, Marina A. Tsvetikova, Tatyana V. Demidkina, Natalia V. Anufrieva, Maria V. Barbolina, S.V. Revtovich, Vitalia V. Kulikova, Paul Gollnick
Publikováno v:
Biochimie. 147
In the spatial structure of tyrosine phenol-lyase, the Ser51 residue is located in the active site of the enzyme. The replacement of Ser51 with Ala by site-directed mutagenesis led to a decrease of the kcat/Km parameter for reactions with l -tyrosine
Autor:
Yaroslav V. Tkachev, Vitalia V. Koulikova, Nicolai G. Faleev, Lyudmila N. Zakomirdina, V. V. Komissarov, Vladimir P. Timofeev, Tatyana V. Demidkina, Marina A. Tsvetikova, Olga I. Gogoleva, Elena A. Morozova
Publikováno v:
Amino Acids. 41:1247-1256
A comparative study of the kinetics and stereospecificity of isotopic exchange of the pro-2R- and pro-2S protons of glycine in (2)H(2)O under the action of tyrosine phenol-lyase (TPL), tryptophan indole-lyase (TIL) and methionine γ-lyase (MGL) was u
Autor:
Radii M. Khomutov, S.V. Revtovich, Marina A. Tsvetikova, Nicolai G. Faleev, M. M. Vorob'ev, Robert S. Phillips, Tatyana V. Demidkina, Elena N. Khurs, Elena A. Morozova, Kirill V. Alferov
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794:1414-1420
We have studied and compared the pH-dependencies of the main kinetic parameters for the α,γ-elimination reactions of methionine γ-lyase (MGL) of Citrobacter intermedius with natural substrate, l -methionine, with its phosphinic analogue, and for
Autor:
Marina A. Tsvetikova, M. M. Vorob'ev, Nicolai G. Faleev, Robert S. Phillips, Lyudmila N. Zakomirdina, Tatyana V. Demidkina, Olga I. Gogoleva
Publikováno v:
Biochimica et biophysica acta. 1844(10)
The interaction of the mutant tryptophan indole-lyase (TIL) from Proteus vulgaris Y72F with the transition state analogue, oxindolyl- l -alanine (OIA), with the natural substrate, l -tryptophan, and with a substrate S-ethyl- l -cysteine was examined.
Autor:
Nicolai G, Faleev, Kirill V, Alferov, Marina A, Tsvetikova, Elena A, Morozova, Svetlana V, Revtovich, Elena N, Khurs, Mikhail M, Vorob'ev, Robert S, Phillips, Tatyana V, Demidkina, Radii M, Khomutov
Publikováno v:
Biochimica et biophysica acta. 1794(10)
We have studied and compared the pH-dependencies of the main kinetic parameters for the alpha,gamma-elimination reactions of methionine gamma-lyase (MGL) of Citrobacter intermedius with natural substrate, l-methionine, with its phosphinic analogue, a