Results 81 to 90 of about 522 (119)

The critical role of <i>hcpR</i> in regulating nitrosative stress defense in <i>Clostridioides difficile</i>. [PDF]

Appl Environ Microbiol
Kalra S, Ayinde TO, Olaitan AO.
europepmc   +1 more source

Genome-wide identification and expression analysis of the class III peroxidase gene family in Medicago sativa. [PDF]

BMC Plant Biol
Wu J, Cheng H, Liu T, Hao Z, Ma Y, Raza A, Yang P.   +6 more
europepmc   +1 more source

Plant Cell Wall Polysaccharide O-Acetyltransferases. [PDF]

Plants (Basel)
Zhong R, Zhou D, Chen L, Rose JP, Wang BC, Ye ZH.   +5 more
europepmc   +1 more source

Global atlas of predicted functional domains in Legionella pneumophila Dot/Icm translocated effectors. [PDF]

Mol Syst Biol
Patel DT, Stogios PJ, Jaroszewski L, Urbanus ML, Sedova M, Semper C, Le C, Takkouche A, Ichii K, Innabi J, Patel DH, Ensminger AW, Godzik A, Savchenko A.   +13 more
europepmc   +1 more source

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.
Leščić Ašler, Ivana, Ivić, Nives, Kovačić, Filip, Schell, Sabrina, Knorr, Janina, Krauss, Ulrich, Wilhelm, Susanne, Kojić-Prodić, Biserka, Jaeger, Karl-Erich   +8 more
openaire   +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%.
Bielen, A, Ćetković, H, Long, PF, Schwab, H, Abramić, M, Vujaklija, D   +5 more
openaire   +4 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

The substrate selectivity of the two homologous SGNH hydrolases from Streptomyces bacteria: Molecular dynamics and experimental study

International Journal of Biological Macromolecules, 2020
Two extracellular enzymes of the SGNH hydrolase superfamily reveal highly homologous 3D structures, but act on different substrates; one is a true phospholipase A1 from Streptomyces albidoflavus (SaPLA1, EC: 3.1.1.32, PDB code: 4HYQ), whereas the promiscuous enzyme from Streptomyces rimosus (SrLip, EC: 3.1.1.3, PDB code: 5MAL) exhibits lipase ...
Maršavelski, Aleksandra, Sabljić, Igor, Sugimori, Daisuke, Kojić-Prodić, Biserka   +3 more
openaire   +4 more sources

Biochemical characterization of Alr1529, a novel SGNH hydrolase variant from Anabaena sp. PCC 7120

Biochimica et Biophysica Acta (BBA) - 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
Kiranmayee, Bakshy, Sathyanarayana N, Gummadi, Narayanan, Manoj   +2 more
openaire   +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 (
Seulgi, Kim, Song Yi, Bae, Seung Joon, Kim, Tri Duc, Ngo, Kyeong Kyu, Kim, T Doohun, Kim   +5 more
openaire   +2 more sources