Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Markus Gütlich"'
Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP11Edited by I. Wilson
Autor:
Gerd Bader, Anja Herrmann, Susanne Schiffmann, Markus Gütlich, Adelbert Bacher, Tarmo Ploom, Thorsten Lemm, Günter Auerbach, Markus Fischer, Robert Huber
Publikováno v:
Journal of Molecular Biology. 312:1051-1057
Tetrahydrobiopterin, the cofactor required for hydroxylation of aromatic amino acids regulates its own synthesis in mammals through feedback inhibition of GTP cyclohydrolase I. This mechanism is mediated by a regulatory subunit called GTP cyclohydrol
Autor:
Andreas Bracher, Nicholas Schramek, Harald Ritz, Eva Götze, Adelbert Bacher, Markus Gütlich, Anja Herrmann, Wolfgang Eisenreich
Publikováno v:
Journal of Biological Chemistry. 273:28132-28141
GTP cyclohydrolase I catalyzes a ring expansion affording dihydroneopterin triphosphate from GTP. [1',2',3',4',5'-13C5, 2'-2H1]GTP was prepared enzymatically from [U-13C6]glucose for use as enzyme substrate. Multinuclear NMR experiments showed that t
Autor:
Wolfgang Rödl, Irmgard Ziegler, Adelbert Bacher, Markus Gütlich, Klaus Witter, Thomas Werner, Dolores J. Cahill
Publikováno v:
Biochemical Journal. 319:27-32
The GTP cyclohydrolase I (GTP-CH) gene of the cellular slime mould Dictyostelium discoideum has been cloned and sequenced. The 855 bp cDNA of this gene contains the open reading frame (ORF) encoding 232 amino acids with a predicted molecular mass of
Publikováno v:
Biochemical Journal. 314:95-101
6-(D-threo-1´,2´-Dihydroxypropylpterin (dictyopterin) has been identified in extracts of growing Dictyostelium discoideum cells [Klein, Thiery and Tatischeff (1990) Eur. J. Biochem. 187, 665–669]. We demonstrate that it originates from GTP by de
Publikováno v:
Biochemical and Biophysical Research Communications. 218:273-279
GTP-cyclohydrolase I is the first enzyme in the biosynthetic pathway leading to folic acid and tetrahydrobiopterin. We determined the complete sequence of the GTP-cyclohydrolase I gene from the yeast Saccharomyces cerevisiae. The gene, which is locat
Autor:
Irmgard Ziegler, Wolfgang Rödl, Klaus Witter, Gerd Katzenmeier, Thomas Wernert, Markus Gütlich, Adelbert Bacher
Publikováno v:
Pteridines, Vol 6, Iss 3, Pp 108-111 (1995)
Summary We have isolated genomic clones that contained the gene for human GTP cyclohydrolase I. One clone containing the 5'-regulatory region of this gene was further analysed. It encompassed the first exon, parts of the first intron and about 2.6kb
Publikováno v:
Chemistrybiology. 20(1)
SummaryLipid translocation from one lipid bilayer leaflet to the other, termed flip-flop, is required for the distribution of newly synthesized phospholipids during membrane biogenesis. However, a dedicated biogenic lipid flippase has not yet been id
Publikováno v:
Journal of Cellular Physiology. 156:12-16
The development of tetrahydrobiopterin synthesis during lectin stimulation of resting human T lymphocytes (Kerler et al. [1989] FEBS Lett., 250:622–624), the interferon-γ induced neopterin production by human monocytes/macrophages (Huber et al. [1
Publikováno v:
BMC Biochemistry
BMC biochemistry, 6:24
BMC Biochemistry, Vol 6, Iss 1, p 24 (2005)
BMC biochemistry, 6:24
BMC Biochemistry, Vol 6, Iss 1, p 24 (2005)
Background Insect cells can serve as host systems for the recombinant expression of eukaryotic proteins. Using this platform, the controlled expression of 15N/13C labelled proteins requires the analysis of incorporation paths and rates of isotope-lab
Autor:
Günter Auerbach, Gerd Bader, Robert Huber, Nicholas Schramek, Markus Fischer, Adelbert Bacher, Andreas Bracher, Markus Gütlich, Wolfgang Eisenreich
Publikováno v:
Chemistry and Biology of Pteridines and Folates ISBN: 9781461353171
GTP cyclohydrolase I catalyzes a ring expansion affording dihydroneopterin triphosphate from GTP (1, 2). The reaction involves the release of C-8 of GTP as formate. The catalytic domain of the human enzyme shows 37% identity with that of Escherichia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fd97cbe0bfe1861b19cae86d675e78dd
https://doi.org/10.1007/978-1-4615-0945-5_28
https://doi.org/10.1007/978-1-4615-0945-5_28