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Epimerase active domain of Pseudomonas aeruginosa AlgG, a protein that contains a right-handed beta-helix (2005)

by S A Douthit, M Dlakic, D E Ohman, M J Franklin
Venue:J Bacteriol
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Review Biomolecular Mechanisms of Pseudomonas aeruginosa and Escherichia coli Biofilm Formation

by Garry Laverty, Sean P. Gorman, Brendan F. Gilmore , 2014
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...ginate polymer by forming a scaffoldsin the periplasm surrounding newly formed polymer molecules [120]. Epimerization of polymerizedsmannuronate residues is controlled by AlgG, a C-5-epimerase enzyme =-=[121]-=-. Acetylation of thesesmannuronate residues also occurs via the enzymes AlgF, AlgJ, and AlgI at O2 and/or O3 positions [122].sAlgF is located in the periplasm. AlgJ is a type II membrane protein with ...

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by Michael J. Franklin, David E. Nivens, Joelt. Weadge, P. Lynne Howell, Michael J. Franklin, P. Lynne Howell, Molecular Structure , 2011
"... Pseudomonas aeruginosa thrives in many aqueous environments and is an opportunis-tic pathogen that can cause both acute and chronic infections. Environmental conditions and host defenses cause differing stresses on the bacteria, and to survive in vastly differ-ent environments, P. aeruginosa must be ..."
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Pseudomonas aeruginosa thrives in many aqueous environments and is an opportunis-tic pathogen that can cause both acute and chronic infections. Environmental conditions and host defenses cause differing stresses on the bacteria, and to survive in vastly differ-ent environments, P. aeruginosa must be able to adapt to its surroundings. One strategy for bacterial adaptation is to self-encapsulate with matrix material, primarily composed of secreted extracellular polysaccharides. P. aeruginosa has the genetic capacity to pro-duce at least three secreted polysaccharides; alginate, Psl, and Pel.These polysaccharides differ in chemical structure and in their biosynthetic mechanisms. Since alginate is often associated with chronic pulmonary infections, its biosynthetic pathway is the best char-acterized. However, alginate is only produced by a subset of P. aeruginosa strains. Most environmental and other clinical isolates secrete either Pel or Psl. Little information is avail-able on the biosynthesis of these polysaccharides. Here, we review the literature on the alginate biosynthetic pathway, with emphasis on recent findings describing the structure of alginate biosynthetic proteins. This information combined with the characterization of the domain architecture of proteins encoded on the Psl and Pel operons allowed us to
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...the C-terminal domain of AlgG has been modeled and is predicted to contain a right-handed β-helix (RHβH) fold, characteristic of proteins with carbohydrate-binding and sugar hydrolase (CASH) domains (=-=Douthit et al., 2005-=-). The structure of the extracellular alginate epimerase, AlgE4 (PDB ID:2PYG), from Azotobacter vinelandii reinforces this prediction (Rozeboom et al., 2008). CASH domain proteins include the pectate ...

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by Iain D. Hay, Zahid Ur Rehman, M. Fata Moradali, Yajie Wang, Bernd H. A. Rehm
"... Alginate is an important polysaccharide used widely in the food, textile, printing and pharmaceutical industries for its viscosifying, and gelling properties. All commercially produced alginates are isolated from farmed brown seaweeds. These algal alginates suffer from heterogeneity in composition a ..."
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Alginate is an important polysaccharide used widely in the food, textile, printing and pharmaceutical industries for its viscosifying, and gelling properties. All commercially produced alginates are isolated from farmed brown seaweeds. These algal alginates suffer from heterogeneity in composition and material properties. Here, we will discuss alginates produced by bacteria; the molecular mechanisms involved in their biosynthesis; and the potential to utilize these bacterially produced or modified alginates for high-value applications where defined material properties are required.
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..., 2003; Jain et al., 2003). The catalytic residues of AlgG reside in a shallow groove situated in a right-handed beta-helix fold, a common motif of carbohydrate-binding and sugarhydrolysing proteins (=-=Douthit et al., 2005-=-). The kinetics of this enzyme have been thoroughly examined, demonFig. 3. Modification of bacterial alginate. Showing the acetylation of the first two M residues at C2 and C3 respectively; and the C5...

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