Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Holger, Neef"'
Autor:
Ralph Golbik, Ronald Kluger, Stephan König, Erik Fiedler, Gerhard Hübner, German A. Kochetov, Kai Tittmann, L. E. Meshalkina, Holger Neef, Tatjana Sandalova, Gunter Schneider
Publikováno v:
FEBS Journal. 272:1326-1342
Transketolase from baker's yeast is a thiamin diphosphate-dependent enzyme in sugar metabolism that reconstitutes with various analogues of the coenzyme. The methylated analogues (4′-methylamino-thiamin diphosphate and N1′-methylated thiamin diph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ea937011404913a65a9395853bf66327
https://doi.org/10.1111/j.1742-4658.2005.04562.x
https://doi.org/10.1111/j.1742-4658.2005.04562.x
Autor:
Holger Neef, Rudolf Friedemann
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1385:245-250
Ab initio calculations on the HF-SCF 6-31g* level were performed on tautomers as well as protonated and deprotonated species of thiamin. Aspects of the proton relay function of the 4′-aminopyrimidine ring in the thiamin catalysis were studied on mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12631c41c195fc6783f1b7382afe9468
https://doi.org/10.1016/s0167-4838(98)00072-7
https://doi.org/10.1016/s0167-4838(98)00072-7
Publikováno v:
Biochemistry. 36:15772-15779
The pyruvate dehydrogenase multienzyme complex from E. coli shows a sigmoidal dependency of the reaction rate on the substrate concentration when product formation is followed in the presence of physiological concentrations of the cofactor thiamin di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e1348f88d71619dad9e8c339eb15e71e
https://doi.org/10.1021/bi971845z
https://doi.org/10.1021/bi971845z
Autor:
Holger Neef, Gerhard Hübner, Dorothee Kern, Kai Tittmann, Christer Wikner, Margrit Killenberg-Jabs, Gunter Schneider, Gunther Kern
Publikováno v:
Science. 275:67-70
The controversial question of how thiamine diphosphate, the biologically active form of vitamin B 1 , is activated in different enzymes has been addressed. Activation of the coenzyme was studied by measuring thermodynamics and kinetics of deprotonati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cf0fffa4e000b9d1a7a8e7eaf716472
https://doi.org/10.1126/science.275.5296.67
https://doi.org/10.1126/science.275.5296.67
Autor:
Alfred Schellenberger, Ralph Golbik, Stephan König, Steffen Eppendorfer, Holger Neef, Karla Lehle, Rainer Jaenicke, Gerhard Hübner
Publikováno v:
Biological Chemistry Hoppe-Seyler. 374:1129-1134
The reconstitution of pyruvate decarboxylase starts with reversible binding of thiamine diphosphate and Mg2(+)-ions to the apoenzyme, followed by a rate-limiting conformational change to the catalytically active holoenzyme. Investigations with diphos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54ea9d4bc531b140d89860967049a3fc
https://doi.org/10.1515/bchm3.1993.374.7-12.1129
https://doi.org/10.1515/bchm3.1993.374.7-12.1129
Autor:
Brigitta Seliger, Gerhard Hübner, Stephan König, Ralph Golbik, Alfred Schellenberger, German A. Kochetov, Holger Neef, L. E. Meshalkina
Publikováno v:
Bioorganic Chemistry. 19:10-17
To answer the question on the mechanistic significance of the pyrimidine moiety of thiamine pyrophosphate (TPP), the two pyridine analogs of TPP ( N 1 -pyridyl-TPP and N 3 -pyridyl-TPP), as well as 4′-deamino-TPP, have been resynthesized and incuba
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ce9a3e9969e875814bd7d04a21aaf2a4
https://doi.org/10.1016/0045-2068(91)90039-r
https://doi.org/10.1016/0045-2068(91)90039-r
Publikováno v:
Liebigs Annalen der Chemie. 1990:913-916
Improved Synthesis of N1-Pyridylthiamine Pyrophosphate, a Coenzymatically Active Analog of Thiamine Pyrophosphate Our previously published synthesis of the N1-pyridyl analog 1b of thiamine pyrophosphate6) is improved resulting in a remarkably higher
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89bdcee57f1030a6570b7532d86f0b56
https://doi.org/10.1002/jlac.1990199001167
https://doi.org/10.1002/jlac.1990199001167
Autor:
Ralph, Golbik, Ludmilla E, Meshalkina, Tatjana, Sandalova, Kai, Tittmann, Erik, Fiedler, Holger, Neef, Stephan, König, Ronald, Kluger, German A, Kochetov, Gunter, Schneider, Gerhard, Hübner
Publikováno v:
The FEBS journal. 272(6)
Transketolase from baker's yeast is a thiamin diphosphate-dependent enzyme in sugar metabolism that reconstitutes with various analogues of the coenzyme. The methylated analogues (4'-methylamino-thiamin diphosphate and N1'-methylated thiamin diphosph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::325503f96f016607f55b56879e99928d
https://pubmed.ncbi.nlm.nih.gov/15752351
https://pubmed.ncbi.nlm.nih.gov/15752351
Publikováno v:
FEBS Letters. 375:220-222
Transketolase catalyzes the transfer of an aldehyde residue from keto sugars to aldo sugars. The intermediate product is dihydroxyethylthiamine pyrophosphate (DHETPP). In the absence of an acceptor substrate, the reaction is stopped at this stage and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a85a7fb6da63967c8a03b32bf484ab33
https://doi.org/10.1016/0014-5793(95)01214-y
https://doi.org/10.1016/0014-5793(95)01214-y
Autor:
Ralph Golbik, Gerhard Hübner, Gunter Schneider, Kai Tittmann, Erik Fiedler, Stephan König, Holger Neef
Publikováno v:
The Journal of biological chemistry. 276(19)
The cleavage of the donor substrate d-xylulose 5-phosphate by wild-type and H263A mutant yeast transketolase was studied using enzyme kinetics and circular dichroism spectroscopy. The enzymes are able to catalyze the cleavage of donor substrates, the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d2791eafd3edf4f803525aab8937c06
https://pubmed.ncbi.nlm.nih.gov/11278369
https://pubmed.ncbi.nlm.nih.gov/11278369