Results 131 to 140 of about 68,716 (153)
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Biotechnology Letters, 2019
We aimed to characterize a novel SGNH (Ser-Gly-Asn-His) family hydrolase from the annotated genome of marine bacteria with new features.A novel esterase Ali5 from Altererythrobacter ishigakiensis has been identified and classified into SGNH family. Ali5 presented a novel GNSL (Gly-Asn-Ser-Leu(X)) motif that differs from the classic GDSL (Gly-Asp-Ser ...
Xiao-Jian Hu, Jixi Li, Heng-Lin Cui
exaly +4 more sources
We aimed to characterize a novel SGNH (Ser-Gly-Asn-His) family hydrolase from the annotated genome of marine bacteria with new features.A novel esterase Ali5 from Altererythrobacter ishigakiensis has been identified and classified into SGNH family. Ali5 presented a novel GNSL (Gly-Asn-Ser-Leu(X)) motif that differs from the classic GDSL (Gly-Asp-Ser ...
Xiao-Jian Hu, Jixi Li, Heng-Lin Cui
exaly +4 more sources
Journal of Molecular Biology, 2003
Escherichia coli thioesterase I (TAP) is a multifunctional enzyme possessing activities of thioesterase, esterase, arylesterase, protease, and lysophospholipase. In particular, TAP has stereoselectivity for amino acid derivative substrates, hence it is useful for the kinetic resolution of racemic mixtures of industrial chemicals.
Su-Chang Lin
exaly +4 more sources
Escherichia coli thioesterase I (TAP) is a multifunctional enzyme possessing activities of thioesterase, esterase, arylesterase, protease, and lysophospholipase. In particular, TAP has stereoselectivity for amino acid derivative substrates, hence it is useful for the kinetic resolution of racemic mixtures of industrial chemicals.
Su-Chang Lin
exaly +4 more sources
Biochemistry
Thermophilic microbial lipases that retain activity under harsh conditions are a highly desirable tool for catalysis in numerous biosynthetic and biotechnological applications.
Kelsey Minium +7 more
semanticscholar +3 more sources
Thermophilic microbial lipases that retain activity under harsh conditions are a highly desirable tool for catalysis in numerous biosynthetic and biotechnological applications.
Kelsey Minium +7 more
semanticscholar +3 more sources
est19 is a gene from Bacillus sp. K91 that encodes a new esterase. A comparison of the amino acid sequence showed that Est19 has typical Ser-Gly-Asn-His (SGNH) family motifs and could be grouped into the SGNH hydrolase family. The Est19 protein was functionally cloned, and expressed and purified from Escherichia coli BL21(DE3).
Tingting Yu +9 more
semanticscholar +3 more sources
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 ...
A. Mølgaard
semanticscholar +2 more sources
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
semanticscholar +5 more sources
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
semanticscholar +5 more sources
Probing Enzyme Promiscuity of SGNH Hydrolases
ChemBioChem, 2010AbstractSeveral hydrolases of the SGNH superfamily, including the lipase SrLip from Streptomyces rimosus (Q93MW7), the acyl‐CoA thioesterase I TesA from Pseudomonas aeruginosa (Q9HZY8) and the two lipolytic enzymes EstA (from P. aeruginosa, O33407) and EstP (from Pseudomonas putida, Q88QS0), were examined for promiscuity.
Leščić Ašler, Ivana +8 more
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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 (1). According to InterPro database (March 2008.), there are 3775 members of this family, with protein sequences originating mainly from genome ...
Kojić-Prodić, Biserka +2 more
openaire +3 more sources
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
openaire +1 more source

