Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Margrit Killenberg-Jabs"'
Publikováno v:
European Journal of Biochemistry. 268:1698-1704
Homomeric pyruvate decarboxylase (E.C 4.1.1.1) from yeast consists of dimers and tetramers under physiological conditions, a K(d) value of 8.1 microM was determined by analytical ultracentrifugation. Dimers and monomers of the enzyme could be populat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b4188b363fe25a43a423398290650f63
https://doi.org/10.1046/j.1432-1327.2001.02044.x
https://doi.org/10.1046/j.1432-1327.2001.02044.x
Publikováno v:
Biochemistry. 36:1900-1905
We investigated the importance of the interaction between the Nl'-atom of the cofactor thiamine diphosphate and glutamic acid residue 51 in pyruvate decarboxylase (EC 4.1. 1.1). The yeast wild type gene PDCl and the respective mutant genes (E51Q and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ba08032fdec05256279d0bdec0396c6
https://doi.org/10.1021/bi961341l
https://doi.org/10.1021/bi961341l
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
Publikováno v:
Biological Chemistry Hoppe-Seyler. 377:313-320
A novel purification procedure was developed for pyruvate decarboxylase (PDC, E.C. 1.1.1.4) from the haploid yeast strain YSH 4.127-1A expressing only one (PDC1) of the three structural genes for PDC. The purified enzyme is homotetrameric with a mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bba273ed1b157f46af0a1b151858e17e
https://doi.org/10.1515/bchm3.1996.377.5.313
https://doi.org/10.1515/bchm3.1996.377.5.313
Publikováno v:
Biophysical chemistry. 96(2-3)
The folding and stability of recombinant homomeric (α-only) pyruvate decarboxylase from yeast was investigated. Different oligomeric states (tetramers, dimers and monomers) of the enzyme occur under defined conditions. The enzymatic activity is used
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49208933eaf2a05bf914bd15a07702b3
https://pubmed.ncbi.nlm.nih.gov/12034445
https://pubmed.ncbi.nlm.nih.gov/12034445
Publikováno v:
European journal of biochemistry. 268(6)
Homomeric pyruvate decarboxylase (E.C 4.1.1.1) from yeast consists of dimers and tetramers under physiological conditions, a K(d) value of 8.1 microM was determined by analytical ultracentrifugation. Dimers and monomers of the enzyme could be populat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a26ae194a05cb7266e2083fbc5653e64
https://pubmed.ncbi.nlm.nih.gov/11248689
https://pubmed.ncbi.nlm.nih.gov/11248689
Autor:
Kai Tittmann, Gunther Kern, Margrit Killenberg-Jabs, Gunter Schneider, Jörg Schäffner, Michael Spinka, Gerhard Hübner, Christer Wikner, Holger Neef, Dorothee Kern, Sandro Ghisla
Publikováno v:
Europe PubMed Central
Activation of the coenzyme ThDP was studied by measuring the kinetics of deprotonation at the C2 carbon of thiamin diphosphate in the enzymes pyruvate decarboxylase, transketolase, pyruvate dehydrogenase complex, pyruvate oxidase, in site-specific mu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6e1ee4ffebda79f692981677509cc49
http://europepmc.org/abstract/med/9655909
http://europepmc.org/abstract/med/9655909
