Degrassi, G

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  • Degrassi, G (2)
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Author's Bibliography

The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity

Degrassi, G; Kojić, Milan; Ljubijankić, G; Venturi, V

(Microbiology Soc, London, 2000)

TY  - JOUR
AU  - Degrassi, G
AU  - Kojić, Milan
AU  - Ljubijankić, G
AU  - Venturi, V
PY  - 2000
UR  - http://intor.torlakinstitut.com/handle/123456789/791
AB  - The Bacillus pumilus gene encoding acetyl xylan esterase tare) was identified and characterized. The axe gene was expressed and the recombinant enzyme produced in Escherichia coli was purified and characterized. The recombinant enzyme displayed similar properties to the acetyl xylan esterase (AXE) from B. pumilus. The AXE primary structure was 76% identical to the cephalosporin C deacetylase of B. subtilis, and 40% to two recently identified AXEs from Thermoanaerobacterium and Thermotoga maritima. These four proteins are of similar sire and represent a new family of esterases having a broad substrate specificity. The recombinant AXE was demonstrated to have activity on several acetylated substrates, including on cephalosporin C.
PB  - Microbiology Soc, London
T2  - Microbiology-Sgm
T1  - The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity
EP  - 1591
SP  - 1585
VL  - 146
DO  - 10.1099/00221287-146-7-1585
ER  - 
@article{
author = "Degrassi, G and Kojić, Milan and Ljubijankić, G and Venturi, V",
year = "2000",
abstract = "The Bacillus pumilus gene encoding acetyl xylan esterase tare) was identified and characterized. The axe gene was expressed and the recombinant enzyme produced in Escherichia coli was purified and characterized. The recombinant enzyme displayed similar properties to the acetyl xylan esterase (AXE) from B. pumilus. The AXE primary structure was 76% identical to the cephalosporin C deacetylase of B. subtilis, and 40% to two recently identified AXEs from Thermoanaerobacterium and Thermotoga maritima. These four proteins are of similar sire and represent a new family of esterases having a broad substrate specificity. The recombinant AXE was demonstrated to have activity on several acetylated substrates, including on cephalosporin C.",
publisher = "Microbiology Soc, London",
journal = "Microbiology-Sgm",
title = "The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity",
pages = "1591-1585",
volume = "146",
doi = "10.1099/00221287-146-7-1585"
}
Degrassi, G., Kojić, M., Ljubijankić, G.,& Venturi, V.. (2000). The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity. in Microbiology-Sgm
Microbiology Soc, London., 146, 1585-1591.
https://doi.org/10.1099/00221287-146-7-1585
Degrassi G, Kojić M, Ljubijankić G, Venturi V. The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity. in Microbiology-Sgm. 2000;146:1585-1591.
doi:10.1099/00221287-146-7-1585 .
Degrassi, G, Kojić, Milan, Ljubijankić, G, Venturi, V, "The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterases with broad substrate specificity" in Microbiology-Sgm, 146 (2000):1585-1591,
https://doi.org/10.1099/00221287-146-7-1585 . .
3
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Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production

Kojić, Milan; Degrassi, G; Venturi, V

(Elsevier, Amsterdam, 1999)

TY  - JOUR
AU  - Kojić, Milan
AU  - Degrassi, G
AU  - Venturi, V
PY  - 1999
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/127
UR  - http://intor.torlakinstitut.com/handle/123456789/722
AB  - The rpoS gene which encodes a stationary phase sigma factor has been identified and characterised from the rhizosphere-colonising plant growth-promoting Pseudomonas putida strain WCS358. The predicted protein sequence has extensive homologies with the RpoS proteins form other bacteria, in particular with the RpoS sigma factors of the fluorescent pseudomonads. A genomic transposon insertion in the rpoS gene was constructed, these mutants were analysed for their ability to produce siderophore (iron-transport agent) and the autoinducer quorum-sensing molecules called homoserine lactones (AHL). It was determined that RpoS was not involved in the regulation of siderophore and AHL production, synthesis of these molecules is important for gene expression at stationary phase. P. putida WCS358 produces at least three different AHL molecules.
PB  - Elsevier, Amsterdam
T2  - Biochimica Et Biophysica Acta-Gene Structure and Expression
T1  - Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production
EP  - 420
IS  - 2-3
SP  - 413
VL  - 1489
DO  - 10.1016/S0167-4781(99)00210-9
ER  - 
@article{
author = "Kojić, Milan and Degrassi, G and Venturi, V",
year = "1999",
abstract = "The rpoS gene which encodes a stationary phase sigma factor has been identified and characterised from the rhizosphere-colonising plant growth-promoting Pseudomonas putida strain WCS358. The predicted protein sequence has extensive homologies with the RpoS proteins form other bacteria, in particular with the RpoS sigma factors of the fluorescent pseudomonads. A genomic transposon insertion in the rpoS gene was constructed, these mutants were analysed for their ability to produce siderophore (iron-transport agent) and the autoinducer quorum-sensing molecules called homoserine lactones (AHL). It was determined that RpoS was not involved in the regulation of siderophore and AHL production, synthesis of these molecules is important for gene expression at stationary phase. P. putida WCS358 produces at least three different AHL molecules.",
publisher = "Elsevier, Amsterdam",
journal = "Biochimica Et Biophysica Acta-Gene Structure and Expression",
title = "Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production",
pages = "420-413",
number = "2-3",
volume = "1489",
doi = "10.1016/S0167-4781(99)00210-9"
}
Kojić, M., Degrassi, G.,& Venturi, V.. (1999). Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production. in Biochimica Et Biophysica Acta-Gene Structure and Expression
Elsevier, Amsterdam., 1489(2-3), 413-420.
https://doi.org/10.1016/S0167-4781(99)00210-9
Kojić M, Degrassi G, Venturi V. Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production. in Biochimica Et Biophysica Acta-Gene Structure and Expression. 1999;1489(2-3):413-420.
doi:10.1016/S0167-4781(99)00210-9 .
Kojić, Milan, Degrassi, G, Venturi, V, "Cloning and characterisation of the rpoS gene from plant growth-promoting Pseudomonas putida WCS358: RpoS is not involved in siderophore and homoserine lactone production" in Biochimica Et Biophysica Acta-Gene Structure and Expression, 1489, no. 2-3 (1999):413-420,
https://doi.org/10.1016/S0167-4781(99)00210-9 . .
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