Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Michael Jaehme"'
Publikováno v:
Molecules, Vol 25, Iss 8, p 1940 (2020)
NadR is a bifunctional enzyme that converts nicotinamide riboside (NR) into nicotinamide mononucleotide (NMN), which is then converted into nicotinamide adenine dinucleotide (NAD). Although a crystal structure of the enzyme from the Gram-negative bac
Externí odkaz:
https://doaj.org/article/06fe186f97f84b458bcfadc50abe8409
Publikováno v:
Journal of general physiology, 150(1):jgp.201711850, 41-50
The Journal of General Physiology
The Journal of General Physiology
The bacterial pyridine nucleotide uptake family of transporters mediates the uptake of B-type vitamins, but their transport mechanism is unknown. Jaehme et al. show that the PnuT thiamine transporter utilizes a facilitated diffusion mechanism and sup
Autor:
Michael Jaehme, Dirk Jan Slotboom
Publikováno v:
Biological Chemistry. 396(9-10):955-966
Many bacteria can take up vitamins from the environment via specific transport machineries. Uptake is essential for organisms that lack complete vitamin biosynthesis pathways, but even in the presence of biosynthesis routes uptake is likely preferred
Publikováno v:
Trends in Biochemical Sciences, 40(4), 183-188. ELSEVIER SCIENCE LONDON
The evolutionary relation between sugar and vitamin transporters from the SWEET and Pnu families is un- clear. They have similar 3D structures, but differ in the topology of their secondary structure elements, and lack significant sequence similarity
Autor:
Dirk Jan Slotboom, Michael Jaehme
Publikováno v:
Biochimica et Biophysica Acta (BBA)-General Subjects
Biochimica et biophysica acta, 1850(3), 565-576
Biochimica et biophysica acta, 1850(3), 565-576
BACKGROUND: All organisms use cofactors to extend the catalytic capacities of proteins. Many bacteria and archaea can synthesize cofactors from primary metabolites, but there are also prokaryotes that do not have the complete biosynthetic pathways fo
Autor:
Eva Bosse-Doenecke, Matthias Brandsch, Fritz Markwardt, Michael Jaehme, Matthias Weiwad, Rainer Rudolph, Madlen Dorn
Publikováno v:
FEBS Letters. 583:1631-1636
In the present study we show in the Xenopus laevis expression system that the proton-coupled amino acid transporter 1 (PAT1, SLC36A1) is glycosylated at asparagine residues N174, N183 and N470. To determine the functional role of N-glycosylation, gly
Publikováno v:
Trends in Biochemical Sciences, 41(2), 117-118. ELSEVIER SCIENCE LONDON
The recent review by Feng and Frommer [1] summarizes spectacular new insights into the molecular architecture of SemiSWEET transporters for sugars, resulting from four crystal structures published over the past 12 months [2–4]. The authors briefly
Publikováno v:
Nature Structural & Molecular Biology, 21(11), 1013-1015. Nature Publishing Group
PnuC transporters catalyze cellular uptake of the NAD(+) precursor nicotinamide riboside (NR) and belong to a large superfamily that includes the SWEET sugar transporters. We present a crystal structure of Neisseria mucosa PnuC, which adopts a highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0645d552f67b601dc38349d2efe41ca
https://research.rug.nl/en/publications/87f12c44-209c-42cf-a2a4-22a3e6395bd5
https://research.rug.nl/en/publications/87f12c44-209c-42cf-a2a4-22a3e6395bd5
Autor:
Hartmut Michel, Michael Jaehme
Publikováno v:
The FEBS journal. 280(4)
Cell-free in vitro synthesis of proteins using coupled transcription/translation is considered to be a powerful alternative to the use of traditional cell-based expression systems. Recently, promising developments have been reported applying cell-fre