Zobrazeno 1 - 10
of 68
pro vyhledávání: '"German A. Kochetov"'
Publikováno v:
Molecular Catalysis. 466:122-129
For baker’s yeast transketolase (TK), cooperative binding of thiamine diphosphate (ThDP) and substrates in the transferase reaction is known. We show here that the differences in the properties of the active centers of TK are formed already upon th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a1aceb3187c673447b07dfd8ccf052a
https://doi.org/10.1016/j.mcat.2019.01.008
https://doi.org/10.1016/j.mcat.2019.01.008
Autor:
Dmitrii S Shcherbinin, Olga N. Solovjeva, German A. Kochetov, Victor G. Zgoda, Maria G. Zavialova, Marina V. Kovina
Publikováno v:
Bioscience Reports
Transketolase catalyzes the transfer of a glycolaldehyde residue from ketose (the donor substrate) to aldose (the acceptor substrate). In the absence of aldose, transketolase catalyzes a one-substrate reaction that involves only ketose. The mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5aae2d4afe10d3a7221011da1832ea28
http://europepmc.org/articles/PMC7403953
http://europepmc.org/articles/PMC7403953
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1832(3):387-390
Until recently it was assumed that the transketolase-like protein (TKTL1) detected in the tumor tissue, is catalytically active mutant form of human transketolase (hTKT). Human TKT shares 61% sequence identity with TKTL1. And the two proteins are 77%
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3c5b5e914f0d6441067004ab5079890
Autor:
Vladimir A. Yurshev, German A. Kochetov, Vitalii A. Selivanov, Olga N. Solovjeva, Irina A. Sevostyanova
Publikováno v:
The Protein Journal. 31:137-140
Catalytic activity has been demonstrated for holotransketolase in the absence of free bivalent cations in the medium. The two active centers of the enzyme are equivalent in both the catalytic activity and the affinity for the substrates. In the prese
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::588ec505854ca0d83d2c2018c3178088
https://doi.org/10.1007/s10930-011-9382-5
https://doi.org/10.1007/s10930-011-9382-5
Publikováno v:
Biochemistry (Moscow). 74:293-300
In this work, we investigated the rate of formation of the central intermediate of the transketolase reaction with thiamine diphosphate (ThDP) or 4'-methylamino-ThDP as cofactors and its stability using stopped-flow spectroscopy and circular dichrois
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb0e25c1c3f571c07b6d0686bb3d6f66
https://doi.org/10.1134/s0006297909030080
https://doi.org/10.1134/s0006297909030080
Publikováno v:
Biochemistry (Moscow). 72:84-92
The two-step mechanism of interaction of thiamine diphosphate (ThDP) with transketolase (TK) has been studied: TK + ThDP ↔ TK ··· ThDP ↔ TK*-ThDP. The scheme involves the formation of inactive intermediate complex TK ··· ThDP followed by it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::275c0f2269b9df17f980ef4a245369ac
https://doi.org/10.1134/s0006297907010105
https://doi.org/10.1134/s0006297907010105
Autor:
Gerhard Hübner, German A. Kochetov, Johanna Brauer, L. E. Meshalkina, Olga Esakova, Ralph Golbik
Publikováno v:
IUBMB Life. 59:104-109
The interaction of thiamine diphosphate (ThDP) with transketolase (TK) involves at least two stages: [formula: see text] During the first stage, an inactive intermediate complex (TK...ThDP) is formed, which is then transformed into a catalytically ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81118ae77635944d367c30440a99e354
https://doi.org/10.1080/15216540701260336
https://doi.org/10.1080/15216540701260336
Autor:
Philip W. Kuchel, German A. Kochetov, Antonio Ramos-Montoya, Marta Cascante, L. E. Meshalkina, Olga N. Solovjeva, Vitaly A. Selivanov, Paul W. N. Lee
Publikováno v:
Bioinformatics. 21:3558-3564
Motivation: Addition of labeled substrates and the measurement of the subsequent distribution of the labels in isotopomers in reaction networks provide a unique method for assessing metabolic fluxes in whole cells. However, owing to insufficiency of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dde6373eb0b0545f715bb67f7f52538
https://doi.org/10.1093/bioinformatics/bti573
https://doi.org/10.1093/bioinformatics/bti573
Publikováno v:
IUBMB Life (International Union of Biochemistry and Molecular Biology: Life). 57:491-497
Transketolase (TK) is a homodimer, the simplest representative of thiamine diphosphate (ThDP)-dependent enzymes. It was first ThDP-dependent enzymes the crystal structure of which has been solved and revealed the general fold for this class of enzyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33ff0fdf7b894036fa0cbc9a008d575a
https://doi.org/10.1080/15216540500167203
https://doi.org/10.1080/15216540500167203
Autor:
E. A. Khanova, L. E. Meshalkina, Gerhard Hübner, Olga Esakova, German A. Kochetov, Ralph Golbik
Publikováno v:
Biochemistry (Moscow). 70:770-776
The influence of transketolase substrates on the interaction of apotransketolase with its coenzyme thiamine diphosphate (TDP) and on the stability of the reconstituted holoenzyme was studied. Donor substrates increased the affinity of the coenzyme fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bf315d0b5f7ac24463e081e0d836516
https://doi.org/10.1007/s10541-005-0182-4
https://doi.org/10.1007/s10541-005-0182-4