Results 91 to 100 of about 522 (119)

SGNH hydrolase-type esterase domain containing Cbes-AcXE2: a novel and thermostable acetyl xylan esterase from Caldicellulosiruptor bescii

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, Sneha S, Sathe, Annamma A, Odaneth, Arvind M, Lali, Sanjeev K, Chandrayan   +4 more
openaire   +2 more sources

How promiscuous are SGNH-hydrolases?

2008
Although 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, Ivić, Nives, Kojić-Prodić, Biserka   +1 more
openaire   +3 more sources

A novel SGNH family hydrolase Ali5 with thioesterase activity and a GNSL motif but without a classic GDSL motif from Altererythrobacter ishigakiensis

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 ...
Li-Guo, Hong, Shu-Ling, Jian, Ying-Yi, Huo, Hong, Cheng, Xiao-Jian, Hu, Jixi, Li, Heng-Lin, Cui, Xue-Wei, Xu   +7 more
openaire   +2 more sources

Catalytic Dyad in the SGNH Hydrolase Superfamily: In-depth Insight into Structural Parameters Tuning the Catalytic Process of Extracellular Lipase from Streptomyces rimosus

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, Zoran Štefanić, Aleksandra Maršavelski, Robert Vianello, Biserka Kojić-Prodić   +4 more
openaire   +4 more sources

Characterization of a Highly Solvent-Tolerant SGNH Hydrolase Superfamily Lipolytic Enzyme from Sphaerobacter thermophilus

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, Zachary J. Knepp, Morgan Sutton, Tabatha Falls, Sara Bobb, Connor McKeefery, Kailynn Smith, Kyle T. Root   +7 more
openaire   +2 more sources

Crystal Structure of Escherichia coli Thioesterase I/Protease I/Lysophospholipase L1: Consensus Sequence Blocks Constitute the Catalytic Center of SGNH-hydrolases through a Conserved Hydrogen Bond Network

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.
Yu-Chih, Lo, Su-Chang, Lin, Jei-Fu, Shaw, Yen-Chywan, Liaw   +3 more
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The SGNH-hydrolases from streptomycetes

2009
Lipases (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, Pigac, Jasenka, Abramić, Marija, Bielen, Ana   +3 more
openaire   +1 more source

Rhamnogalacturonan Acetylesterase, a Member of the SGNH-Hydrolase Family

2003
Rhamnogalacturonan 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 ...
openaire   +1 more source

Bioinformatics Approach to Characterisation of SGNH Hydrolase

2005
The 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
openaire  

Discovery of a Ni2+-dependent guanidine hydrolase in bacteria

Nature, 2022
Dietmar Funck, Malte Sinn, Jennifer Fleming   +2 more
exaly