Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Lyudmila N. Zakomirdina"'
Autor:
Dalibor Milić, Alfred A. Antson, Lyudmila N. Zakomirdina, Dubravka Matković-Čalogović, Tatyana V. Demidkina
Publikováno v:
Croatica Chemica Acta
Volume 85
Issue 3
Volume 85
Issue 3
Tyrosine phenol-lyase (TPL) is a pyridoxal-5′-phosphate (PLP) dependent enzyme which catalyzes β-elimination of L-tyrosine. In the holoenzyme the protonated pyridinium N1 atom of the PLP cofactor is hydrogen-bonded to the side chain of Asp214. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58ff0ba7e7a9eaee03fc088ea6c9b54e
https://doi.org/10.5562/cca1915
https://doi.org/10.5562/cca1915
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
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18630d5627e59bd1429440fbcd6710fd
https://doi.org/10.1007/s00726-010-0802-1
https://doi.org/10.1007/s00726-010-0802-1
Autor:
Luca Ronda, Tatyana V. Demidkina, Robert S Phillips, Lyudmila N. Zakomirdina, Nicolai G Faleev, Irene S. Dementieva, Vitalia V. Kulikova, Andrea Mozzarelli, Paul Gollnick
Publikováno v:
Biochemistry. 42:11161-11169
Tryptophan indole-lyase (Trpase) from Proteus vulgaris is a pyridoxal 5'-phosphate dependent enzyme that catalyzes the reversible hydrolytic cleavage of L-Trp to yield indole and ammonium pyruvate. Asp-133 and His-458 are strictly conserved in all se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd014655ea19b80cd0e65760679347d0
https://doi.org/10.1021/bi034348t
https://doi.org/10.1021/bi034348t
Autor:
Tatyana V. Demidkina, Lyudmila N. Zakomirdina, Robert S. Phillips, Olga I. Gogoleva, N. G. Faleev
Publikováno v:
Enzyme and Microbial Technology. 32:843-850
To shed light on the mechanism of hydrophobic control in reactions of microbial tryptophanase the direct effect of the solvent hydrophobicity on affinities of amino acid inhibitors was first examined. Values of inhibition constants ( K i ) for a vari
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::36a6b033c3d832eceeac9efc321e6ff9
https://doi.org/10.1016/s0141-0229(03)00057-7
https://doi.org/10.1016/s0141-0229(03)00057-7
Autor:
Stefano Bruno, Luca Ronda, Andrea Mozzarelli, Tatyana V. Demidkina, Robert S. Phillips, Lyudmila N. Zakomirdina
Publikováno v:
Journal of Biological Chemistry. 277:21592-21597
The binding of substrates and inhibitors to wild-type Proteus vulgaris tryptophan indole-lyase and to wild type and Y71F Citrobacter freundii tyrosine phenol-lyase was investigated in the crystalline state by polarized absorption microspectrophotomet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a16682302ed3f7e4310d5b4b2b121559
https://doi.org/10.1074/jbc.m200216200
https://doi.org/10.1074/jbc.m200216200
Autor:
Lyudmila N. Zakomirdina, N. G. Faleev, I. S. Dementieva, Olga I. Gogoleva, Tatyana V. Demidkina, Vitalia V. Kulikova
Publikováno v:
Biochemistry (Moscow). 67:1189-1196
An efficient method for purification of recombinant tryptophanase from Proteus vulgaris was developed. Catalytic properties of the enzyme in reactions with L-tryptophan and some other substrates as well as competitive inhibition by various amino acid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::044fe6737302eadc325f1f696eb12b4e
https://doi.org/10.1023/a:1020975610046
https://doi.org/10.1023/a:1020975610046
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.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95021a83ac4a9ac2e9c334f6e4a675a3
https://pubmed.ncbi.nlm.nih.gov/25084024
https://pubmed.ncbi.nlm.nih.gov/25084024
Autor:
Andrey Lebedev, Alfred A. Antson, Keith S. Wilson, Eleanor J. Dodson, Zbigniew Dauter, Guy Dodson, Irene S. Dementieva, E.H. Harutyunyan, Lyudmila N. Zakomirdina, Michail N. Isupov
Publikováno v:
Journal of Molecular Biology. 276:603-623
The X-ray structure of tryptophanase (Tnase) reveals the interactions responsible for binding of the pyridoxal 5'-phosphate (PLP) and atomic details of the K+ binding site essential for catalysis. The structure of holo Tnase from Proteus vulgaris (sp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e78c4fb6a3d3ac3f91a128d656a404c6
https://doi.org/10.1006/jmbi.1997.1561
https://doi.org/10.1006/jmbi.1997.1561
Publikováno v:
European Journal of Biochemistry. 193:243-247
Tryptophanase from Escherichia coli was oriented in a compressed slab of polyacrylamide gel and its linear dichroism (LD) and absorption spectra have been measured. The free enzyme displays four LD bands at 305, 340, 425 and 490 nm. Two bands at 340
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f946507a19bd384fd36769ed31655346
https://doi.org/10.1111/j.1432-1033.1990.tb19329.x
https://doi.org/10.1111/j.1432-1033.1990.tb19329.x
Autor:
Paul Gollnick, Bazhulina Np, I. S. Dementieva, N. G. Faleev, Vitalia V. Kulikova, Tatyana V. Demidkina, Lyudmila N. Zakomirdina
Publikováno v:
Biochemistry. Biokhimiia. 68(11)
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 coenzyme. The replacement of arginine 226 with alanine using site-directed mutagenesis reduced th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c320b914453e66ead7fbbf121f95054
https://pubmed.ncbi.nlm.nih.gov/14640959
https://pubmed.ncbi.nlm.nih.gov/14640959