Results 111 to 120 of about 34,392 (132)

Probing Enzyme Promiscuity of SGNH Hydrolases

ChemBioChem, 2010
AbstractSeveral 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.
Filip Kovacic, Biserka Kojić-Prodić, Ivana Leščić Ašler   +2 more
exaly   +3 more sources

Uncharacterized DUF1574 Leptospira Proteins Are SGNH Hydrolases [PDF]

Cell Cycle, 2008
Leptospira borgpetersenii and Leptospira interrogans are nonsporulating bacteria responsible for leptospirosis, which is presumed to be the most widespread zoonosis in the world. This water-borne pathogen is usually transmitted to humans through the contact with contaminated soil or water, via infected animal tissue or rat bites. Consequently, farmers,
Dariusz Plewczynski, Kamil Steczkiewicz, Andrzej Koliński   +2 more
exaly   +3 more sources

Visualization of a Substrate-Induced Productive Conformation of the Catalytic Triad of the Neisseria meningitidis Peptidoglycan O-Acetylesterase Reveals Mechanistic Conservation in SGNH Esterase Family Members

Acta Crystallographica Section D: Biological Crystallography, 2014
International audiencePeptidoglycan O-acetylesterase (Ape1), which is required for host survival in Neisseria sp., belongs to the diverse SGNH hydrolase superfamily, which includes important viral and bacterial virulence factors.
Ivo G Boneca, Stephen W White, Muhamed-Kheir Taha   +2 more
exaly   +2 more sources

The SGNH-Hydrolase of Streptomyces Coelicolor Has (Aryl)Esterase and a True Lipase Activity

Biochimie, 2009
The Streptomyces coelicolor A3(2) gene SCI11.14c was overexpressed and purified as a His-tagged protein from heterologous host, Streptomyces lividans. The purification procedure resulted in 34.1-fold increase in specific activity with an overall yield of 21.4%.
Paul F. Long, Dus̆Ica Vujaklija, Helmut Schwab   +2 more
exaly   +5 more sources

Bioinformatics Approach to Characterization of SGNH/GDSL-Hydrolases [PDF]

Acta Crystallographica Section A: Foundations and Advances, 2005
B Kojić-Prodić
exaly   +2 more sources

Characterization, Amyloid Formation, and Immobilization of a Novel SGNH Hydrolase From Listeria innocua 11262

International Journal of Biological Macromolecules, 2012
A novel oligomeric hydrolase (LI22) from Listeria innocua CLIP 11262 was identified, characterized, and immobilized for industrial application. Sequence analysis of LI22 revealed a putative catalytic triad (Ser(10)-Asp(176)-His(179)), and a conserved sequence motif Ser(S)(10)-Gly(G)(77)-Asn(N)(79)-His(H)(179) with moderate identities (
Tri D Ngo, Kyeong Kyu Kim, T Doohun Kim
exaly   +3 more sources

Biochemical Characterization of Alr1529, a Novel SGNH Hydrolase Variant From Anabaena sp. PCC 7120

Biochimica Et Biophysica Acta - Proteins and Proteomics, 2009
Alr1529, a serine hydrolase from the cyanobacteria Anabaena sp. strain PCC 7120 is a member of the SGNH hydrolase superfamily. Biochemical characterization of the purified enzyme revealed that the protein is a dimer in solution and is specific for aryl esters of short chain carboxylic acids. The enzyme was regio-selective for alpha-naphthyl esters with
Sathyanarayana N. Gummadi, Manoj Narayanan   +1 more
exaly   +3 more sources

Characterization and immobilization of a novel SGNH hydrolase (Est24) from Sinorhizobium meliloti

Applied Microbiology and Biotechnology, 2012
A novel oligomeric SGNH hydrolase (Est24) from Sinorhizobium meliloti was identified, actively expressed in Escherichia coli, characterized, and immobilized for industrial application. Sequence analysis of Est24 revealed a putative catalytic triad (Ser¹³-Asp¹⁶³-His¹⁶⁹), with moderate homology to other SGNH hydrolases. Est24 was more active toward short-
Song Yi, Bae, Bum Han, Ryu, Eunjin, Jang, Seulgi, Kim, T Doohun, Kim   +4 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.
Jei-Fu Shaw, Su-Chang Lin, Yen-Chywan Liaw   +2 more
exaly   +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 ...
Xiao Jian Hu, Heng-Lin Cui, Jixi Li
exaly   +3 more sources