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Structure of the histidine-containing phosphocarrier protein HPr from Bacillus subtilis at 2.0-A resolution

Autor: S. L. Sutrina, Osnat Herzberg, Jonathan Reizer, Milton H. Saier, Prasad T. Reddy, Geeta Kapadia

Publikováno v: Proceedings of the National Academy of Sciences. 89:2499-2503

The crystal structure of the histidine-containing phosphocarrier protein (HPr) of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Bacillus subtilis has been determined at 2.0-A resolution and refined to a crystallographic residual

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9278e431c6af80fd9bdf0b0b06b21427
https://doi.org/10.1073/pnas.89.6.2499

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Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy

Autor: Arthur G. Palmer, John Cavanagh, Wayne J. Fairbrother, H.J. Dyson, Milton H. Saier, S. L. Sutrina, Jonathan Reizer, Peter E. Wright

Publikováno v: Biochemistry. 30:6896-6907

The enzyme IIIglc-like domain of Bacillus subtilis IIglc (IIIglc, 162 residues, 17.4 kDa) has been cloned and overexpressed in Escherichia coli. Sequence-specific assignment of the backbone 1H and 15N resonances has been carried out with a combinatio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::160d2b541086119d1b023c4d15f247af
https://doi.org/10.1021/bi00242a013

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The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease

Autor: Jonathan Reizer, Milton H. Saier, Prasad T. Reddy, S. L. Sutrina

Publikováno v: Journal of Biological Chemistry. 265:18581-18589

Biochemical, immunological, and sequence analyses demonstrated that the glucose permease of Bacillus subtilis, the glucose-specific Enzyme II of the phosphoenolpyruvate-dependent phosphotransferase system, is a single polypeptide chain with a C-termi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::9cd0cde2bd8324a0035956b2f3428e42
https://doi.org/10.1016/s0021-9258(17)44791-0

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Identification of catalytic residues in the beta-glucoside permease of Escherichia coli by site-specific mutagenesis and demonstration of interdomain cross-reactivity between the beta-glucoside and glucose systems

Autor: Bodo Rak, S L Sutrina, Karin Schnetz, Milton H. Saier

Publikováno v: Journal of Biological Chemistry. 265:13464-13471

beta-Glucoside Enzyme II (IIBgl) of the Escherichia coli phosphotransferase system transports and phosphorylates beta-glucosides, whereas the glucose Enzyme II-III pair (IIGlc-IIIGlc) transports and phosphorylates glucose as well as certain aliphatic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b470f8a84ffc9840c9a586cfb2d4d8a1
https://doi.org/10.1016/s0021-9258(18)77370-5

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Mechanism of sugar transport and phosphorylation via permeases of the bacterial phosphotransferase system: Catalytic residues in the β-glucoside-specific permease as defined by site-specific mutagenesis

Autor: S. L. Sutrina, Milton H. Saier, Karin Schnetz, Bodo Rak

Publikováno v: Research in Microbiology. 141:368-374

The mechanism of action of the β-glucoside permease (IIbgl) of the Escherichia coli phosphotransferase system (PTS) was investigated employing site-specific mutagenesis and a variety of kinetic approaches. The enzyme catalyses three phosphoryl trans

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66bd5540add21955b4965b5e65919fea
https://doi.org/10.1016/0923-2508(90)90014-h

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Contents Vol. 12, 2007

Publikováno v: Journal of Molecular Microbiology and Biotechnology. 12:277-278

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c82acb8a1ca385612ec1fde14180ee67
https://doi.org/10.1159/000104694

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Functional interactions between proteins of the phosphoenolpyruvate:sugar phosphotransferase systems of Bacillus subtilis and Escherichia coli

Autor: J, Reizer, S L, Sutrina, L F, Wu, J, Deutscher, P, Reddy, M H, Saier

Publikováno v: The Journal of biological chemistry. 267(13)

Proteins of the phosphoenolpyruvate:sugar phosphotransferase system (PTS) of Bacillus subtilis were overexpressed, purified to near homogeneity, and characterized. The proteins isolated include Enzyme I, HPr, the glucose-specific IIA domain of the gl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::b151be4b1f47d8c6b7060c3e7253379d
https://pubmed.ncbi.nlm.nih.gov/1577753

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Crystallization and preliminary X-ray analysis of the lactose-specific phosphocarrier protein IIAlac of the phosphoenolpyruvate: sugar phosphotransferase system from Staphylococcus aureus

Autor: Milton H. Saier, George C. Stewart, Jonathan Reizer, Reha Celikel, Nguyen-Huu Xuong, Xiaoping Dai, S. L. Sutrina

Publikováno v: Journal of molecular biology. 222(4)

The IIA constituent of the lactose permease from Staphylococcus aureus has been crystallized in two different forms. Crystals of form I have been grown from polyethylene glycol 4000 with beta-octyl glucoside. They diffract to 3.0 A resolution and bel

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5779fe49dbd51fe5051b67fb9038e60d
https://pubmed.ncbi.nlm.nih.gov/1762152

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The glucose permease of Bacillus subtilis is a single polypeptide chain that functions to energize the sucrose permease

Autor: S L, Sutrina, P, Reddy, M H, Saier, J, Reizer

Publikováno v: The Journal of biological chemistry. 265(30)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e9e20751e21def41178fe16dfe001a53
https://pubmed.ncbi.nlm.nih.gov/2120236

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