Zobrazeno 1 - 10
of 36
pro vyhledávání: '"ENZYME-IIMTL"'
Stoichiometry and Substrate Affinity of the Mannitol Transporter, EnzymeIImtl, from Escherichia coli
Publikováno v:
Biophysical Journal, 89(1), 201-210. CELL PRESS
Uptake and consecutive phosphorylation of mannitol in Escherichia coli is catalyzed by the mannitol permease EnzymeIImtl. The substrate is bound at an extracellular-oriented binding site, translocated to an inward-facing site, from where it is phosph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de99d6d7f1ab11b944af928213e77d92
https://doi.org/10.1529/biophysj.105.062877
https://doi.org/10.1529/biophysj.105.062877
Publikováno v:
Biophysical Journal, 86(4), 1959-1968. CELL PRESS
Flow dialysis has found widespread use in determining the dissociation constant (K-D) of a protein-ligand interaction or the amount of available binding sites (E-0). This method has the potency to measure both these parameters in a single experiment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44f1b6c478c2564c47896f721a37da9f
Autor:
Jaap Broos, Gea K. Schuurman-Wolters, Joyce Wind, George T. Robillard, Bart A. van Montfort, Bert Poolman
Publikováno v:
The Journal of Biological Chemistry, 277(17), 14717-14723. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
A cysteine cross-linking approach was used to identify residues at the dimer interface of the Escherichia coli mannitol permease. This transport protein comprises two cytoplasmic domains and one membrane-embedded C domain per monomer, of which the la
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3bb76ef14430493b07038e77f8875ca0
https://doi.org/10.1074/jbc.m201533200
https://doi.org/10.1074/jbc.m201533200
Autor:
Berend Poolman, Ria H. Duurkens, R. Mensen, B.A. van Montfort, Gea K. Schuurman-Wolters, G.T. Robillard
Publikováno v:
The Journal of Biological Chemistry, 276(16), 12756-12763. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Part of the dimer and B/C domain interface of the Escherichia coli mannitol permease (EII(mtl)) has been identified by the generation of disulfide bridges in a single-cysteine EII(mtl), with only the activity linked Cys(384) in the B domain, and in a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fbed26e8f50c29ee4e5650ab909605c
https://hdl.handle.net/11370/a3198853-ca47-4bf2-8989-d28ce389d765
https://hdl.handle.net/11370/a3198853-ca47-4bf2-8989-d28ce389d765
Publikováno v:
Biochemical Society Transactions. 26(3):532-538
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dris___01423::cf2a7fbfbcccc8ca7555d00d024e97eb
https://research.rug.nl/en/publications/130782dc-17e5-412f-888f-4237f0c9fca4
https://research.rug.nl/en/publications/130782dc-17e5-412f-888f-4237f0c9fca4
Publikováno v:
The Journal of Biological Chemistry. 273(33):20785-20794
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=dris___01423::ecd8f361271f786240d4e849dd9193f3
https://doi.org/10.1074/jbc.273.33.20785
https://doi.org/10.1074/jbc.273.33.20785
Publikováno v:
Biochimica et Biophysica Acta-Biomembranes, 1818(3), 861-868. Elsevier
The mannitol transporter EIImtl from Escherichia coli is responsible for the uptake of mannitol over the inner membrane and its concomitant phosphorylation. EIImtl is functional as a dimer and its membrane-embedded C domain, IICmtl, harbors one high
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::459ea11f8b488e5136589683a44c68d9
https://pubmed.ncbi.nlm.nih.gov/22100747
https://pubmed.ncbi.nlm.nih.gov/22100747
Publikováno v:
The Journal of Biological Chemistry, 285(33), 25324-25331. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
The mannitol transporter from Escherichia coli, EII(mtl), belongs to a class of membrane proteins coupling the transport of substrates with their chemical modification. EII(mtl) is functional as a homodimer, and it harbors one high affinity mannitol-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cb10a206116c2300599a08b88a8b274
https://europepmc.org/articles/PMC2919095/
https://europepmc.org/articles/PMC2919095/
Autor:
Margherita Gonnelli, Michel Koolhof, Erwin P. P. Vos, Jaap Broos, George T. Robillard, Giovanni B. Strambini
Publikováno v:
Biochemistry, 39(35), 10877-10883. AMER CHEMICAL SOC
This paper presents a tryptophan phosphorescence spectroscopy study on the membrane-bound mannitol transporter, EII(mtl), from E. coli. The protein contains four tryptophans at positions 30, 42, 109, and 117. Phosphorescence decays in buffer at 1 deg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b969f1ae9569e8588e1eb52cb4c85189
https://research.rug.nl/en/publications/4df35704-53e4-40d4-a81a-59060881f3f7
https://research.rug.nl/en/publications/4df35704-53e4-40d4-a81a-59060881f3f7
Publikováno v:
Biochemistry, 38(31), 9798-9803. AMER CHEMICAL SOC
This paper presents a deceptively straightforward experimental approach to monitoring membrane protein-ligand interactions in vesicles and in living Escherichia coli cells. This is achieved via the biosynthetic incorporation of 7-azatryptophan, a try
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b78edb1626f302391ee53a5cbd375a41
https://pubmed.ncbi.nlm.nih.gov/10433685
https://pubmed.ncbi.nlm.nih.gov/10433685