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Comparison of cell wall proteins of Saccharomyces cerevisiae as anchors for cell surface expression of heterologous proteins

Article Abstract:

The carboxyl-terminal regions of Cwp1p, Cwp2p, Ag-alpha-1p, Tip1p and Flo1p cell wall proteins, and Sed1p, YCR89w and Tir1p potential cell wall proteins can immobilize alpha-galactosidase in the Saccharomyces cerevisiae cell wall. The degree of anchoring is independent of the length of the C-terminal region. Maximum localization of the fusion galactosidase proteins occurs when Cwp2p, Ag-alpha-1p or Sed1p are used as anchors. Alpha-galactosidase immobilized by the carboxyl-terminal of Cwp2p, is effective in the hydrolysis of guar gum of Cyamopsis tetragonoloba.

Author: Klis, Frans M., Verrips, C. Theo, Chapman, John W., Van Der Vaart, J. Marcel, Te Biesebeke, Rob, Toschka, Holger Y.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
Physiological aspects, Observations, Membrane proteins, Saccharomyces, Bacterial cell walls

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Cloning of the Pseudomonas glumae lipase gene and determination of active site residues

Article Abstract:

Theisolation and characterization of the Pseudomonas glumae lipase gene is discussed. The catalytic site of this lipase, the Ser-Asp-His triad, was determined while putative active site residues were located in conserved areas.Substitution mutants for conserved Ser, Asp and His residues were constructed to determine the involvement of residues in the catalysis. From this method, itwas found that the catalytic triad of the P. glumae lipase is composed of Ser-87, Asp-241 and His-285.

Author: Verrips, C. Theo, Frenken, Leon G.J., Egmond, Maarten R., Batenburg,A. Max, Bos, J. Wil, Visser, Chris
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1992
Binding sites (Biochemistry), Active sites (Biochemistry), Lipase

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Cloning of a mineral phosphate-solubilizing gene from Pseudomonas cepacia

Article Abstract:

Expression of a functional mineral phosphate-solubilizing gene gabY from Pseudomonas cepacia in Escherichia coli JM109 stimulates the dissolution of exogenous hydroxyapatite and production of gluconic acid. Experimental studies reveal the presence of a single open reading frame in the gene. The nucleotide sequence of gabY codes for a protein GabY, whose molecular weight is 14.235 kDa.

Author: Rogers, Robert D., Goldstein, Alan H., Babu-Khan, Safura, Yeo, Tiong Chia, Martin, Warham L., Duron, Manuel R.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
Escherichia coli, Microbial metabolism

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Subjects list: Research, Analysis, Genetic aspects, Pseudomonas
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