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How promiscuous are SGNH-hydrolases?
2008Although lipolytic enzymes are known for decades, the classification of this type of enzymes is a continuous process. Among many defined classes and families, a new one was recently identified: SGNH-hydrolases. According to InterPro database (June 2008.), there are 3775 members of this family, with protein sequences originating mainly from genome ...
Leščić Ašler, Ivana +1 more
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Extremophiles, 2017
Caldicellulosiruptor bescii, the most thermophilic cellulolytic bacterium, is rich in hydrolytic and accessory enzymes that can degrade untreated biomass, but the precise role of many these enzymes is unknown. One of such enzymes is a predicted GDSL lipase or esterase encoded by the locus Athe_0553.
Surabhi, Soni +4 more
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Caldicellulosiruptor bescii, the most thermophilic cellulolytic bacterium, is rich in hydrolytic and accessory enzymes that can degrade untreated biomass, but the precise role of many these enzymes is unknown. One of such enzymes is a predicted GDSL lipase or esterase encoded by the locus Athe_0553.
Surabhi, Soni +4 more
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Rhamnogalacturonan Acetylesterase, a Member of the SGNH-Hydrolase Family
2003Rhamnogalacturonan acetylesterase (RGAE) from Aspergillus aculeatus acts in synergy with rhamnogalacturonases on the enzymatic degradation of rhamnogalacturonan I (RG-I). RGAE is a member of the Carbohydrate Esterase Family 12 (CEF 12), which also includes two pectin acetylesterases, a cephalosporin C deacetylase and a number of bacterial proteins of ...
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ACS Chemical Biology, 2017
SrLip is an extracellular enzyme from Streptomyces rimosus (Q93MW7) exhibiting lipase, phospholipase, esterase, thioesterase, and tweenase activities. The structure of SrLip is one of a very few lipases, among the 3D-structures of the SGNH superfamily of hydrolases, structurally characterized by synchrotron diffraction data at 1.75 Å resolution (PDB ...
Ivana Leščić Ašler +4 more
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SrLip is an extracellular enzyme from Streptomyces rimosus (Q93MW7) exhibiting lipase, phospholipase, esterase, thioesterase, and tweenase activities. The structure of SrLip is one of a very few lipases, among the 3D-structures of the SGNH superfamily of hydrolases, structurally characterized by synchrotron diffraction data at 1.75 Å resolution (PDB ...
Ivana Leščić Ašler +4 more
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Biochemistry
Thermophilic microbial lipases that retain activity under harsh conditions are a highly desirable tool for catalysis in numerous biosynthetic and biotechnological applications. In this study, a putative SGNH lipase gene, from Sphaerobacter thermophilus (StSGNH1), was overexpressed using a pMCSG7 plasmid in BL21(DE3) cells.
Kelsey Minium +7 more
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Thermophilic microbial lipases that retain activity under harsh conditions are a highly desirable tool for catalysis in numerous biosynthetic and biotechnological applications. In this study, a putative SGNH lipase gene, from Sphaerobacter thermophilus (StSGNH1), was overexpressed using a pMCSG7 plasmid in BL21(DE3) cells.
Kelsey Minium +7 more
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The SGNH-hydrolases from streptomycetes
2009Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) are hydrolytic enzymes widely distributed in microorganisms, plants and animals. Microbial lipases from a wide range of species have been subject of many important studies in the past few years because of the large number of reactions they catalyze.
Vujaklija, Dušica +3 more
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Bioinformatics Approach to Characterisation of SGNH Hydrolase
2005The present analysis is aimed to recognize structural elements of SGNH/GDSL family of enzymes with a novel folding type using bioinformatics tools on data of primary and secondary structures. Out of 770 proteins sequences deposited, data of seven different structures of GDSL hydrolases are solved, only ; those of the best resolution were selected among
Kojić-Prodić, Biserka, Tomić, Sanja
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Characterization and Immobilization of a Novel SGNH Hydrolase (Est24) From Sinorhizobium meliloti
Applied Microbiology and Biotechnology, 2013Eunjin Jang, Bum Han Ryu, T Doohun Kim
exaly
Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature, 2015
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