Zobrazeno 1 - 10 of 230 pro vyhledávání: '"G T Robillard"'
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The Bacillus stearothermophilus mannitol regulator, MtlR, of the phosphotransferase system. A DNA-binding protein, regulated by HPr and iicbmtl-dependent phosphorylation
Autor: S A, Henstra, M, Tuinhof, R H, Duurkens, G T, Robillard
Publikováno v: The Journal of biological chemistry. 274(8)
D-Mannitol is taken up by Bacillus stearothermophilus and phosphorylated via a phosphoenolpyruvate-dependent phosphotransferase system (PTS). The genes involved in the mannitol uptake were recently cloned and sequenced. One of the genes codes for a p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ec55d81d880e9e155977aa0b5dfb58aa
https://pubmed.ncbi.nlm.nih.gov/9988713
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5
The thermal stability and domain interactions of the mannitol permease of Escherichia coli. A differential scanning calorimetry study
Autor: W, Meijberg, G K, Schuurman-Wolters, H, Boer, R M, Scheek, G T, Robillard
Publikováno v: The Journal of biological chemistry. 273(33)
The thermal stability and domain interactions in the mannitol transporter from Escherichia coli, enzyme IImtl, have been studied by differential scanning calorimetry. To this end, the wild type enzyme, IICBAmtl, as well as IICBmtl and IICmtl, were re
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d52e27f6cbedf0e30f071e91ebc691ea
https://pubmed.ncbi.nlm.nih.gov/9694823
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6
Structure characterization of the central repetitive domain of high molecular weight gluten proteins. I. Model studies using cyclic and linear peptides
Autor: A A, Van Dijk, L L, Van Wijk, A, Van Vliet, P, Haris, E, Van Swieten, G I, Tesser, G T, Robillard
Publikováno v: Protein science : a publication of the Protein Society. 6(3)
The high molecular weight (HMW) proteins from wheat contain a repetitive domain that forms 60-80% of their sequence. The consensus peptides PGQGQQ and GYYPTSPQQ form more than 90% of the domain; both are predicted to adopt beta-turn structure. This p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e6545c6df8b022b9fd1794459f927449
https://pubmed.ncbi.nlm.nih.gov/9070446
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7
Phosphorylation-induced torsion-angle strain in the active center of HPr, detected by NMR and restrained molecular dynamics refinement
Autor: N A, Van Nuland, J A, Wiersma, D, Van Der Spoel, B L, De Groot, R M, Scheek, G T, Robillard
Publikováno v: Protein science : a publication of the Protein Society. 5(3)
The structure of the phosphorylated form of the histidine-containing phosphocarrier protein HPr from Escherichia coli has been solved by NMR and compared with that of unphosphorylated HPr. The structural changes that occur upon phosphorylation of His
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ebe5bba81478b798b47168301a4dd4d9
https://pubmed.ncbi.nlm.nih.gov/8868480
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8
Expression, purification, and kinetic characterization of the mannitol transport domain of the phosphoenolpyruvate-dependent mannitol phosphotransferase system of Escherichia coli. Kinetic evidence that the E. coli mannitol transport protein is a functional dimer
Autor: H, Boer, R H, ten Hoeve-Duurkens, G K, Schuurman-Wolters, A, Dijkstra, G T, Robillard
Publikováno v: The Journal of biological chemistry. 269(27)
The overexpression of the membrane-bound C domain of the mannitol transport protein EIIMtl of Escherichia coli has been achieved. This protein, IICMtl, consisting of the first 346 amino acids, was purified from membrane vesicles and still bound manni
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cc4a5e84c2afe9a9167da87e4dc2e136
https://pubmed.ncbi.nlm.nih.gov/8027040
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9
Steady state kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the Escherichia coli phosphoenolpyruvate-dependent phosphotransferase system
Autor: J S, Lolkema, R H, ten Hoeve-Duurkens, G T, Robillard
Publikováno v: The Journal of biological chemistry. 268(24)
The kinetics of mannitol phosphorylation catalyzed by enzyme IImtl of the bacterial P-enolpyruvate-dependent phosphotransferase system are described for three different physical conditions of the enzyme, (i) embedded in the membrane of inside-out (IS
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bfb4cec85934880366bad4af83ec8406
https://pubmed.ncbi.nlm.nih.gov/8349668
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10
31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Escherichia coli phosphotransferase system EIIMtl
Autor: H H, Pas, G H, Meyer, W H, Kruizinga, K S, Tamminga, R P, van Weeghel, G T, Robillard
Publikováno v: The Journal of biological chemistry. 266(11)
The mannitol-specific phosphotransferase system transport protein, Enzyme IIMtl, contains two catalytically important phosphorylated amino acid residues, both present on the cytoplasmic part of the enzyme. Recently, this portion has been subcloned, p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dbdc7623218eccb02a323e342b924f5c
https://pubmed.ncbi.nlm.nih.gov/2016284
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