Výsledky vyhledávání - "Rosa L. Segura"

The transmembrane domain of the T4SS coupling protein TrwB and its role in protein–protein interactions

Autor: Rosa L. Segura, Begoña Ugarte-Uribe, Ana J. Vecino, Félix M. Goñi, Itziar Alkorta, Fernando de la Cruz, Sandra Águila-Arcos

Publikováno v: Biochimica et Biophysica Acta (BBA)-Biomembranes; Vol 1828
Digital.CSIC. Repositorio Institucional del CSIC
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Bacteria use type IV secretion systems to transfer genetic material and proteins from donor to recipient cells, using proteins encoded by conjugative plasmids. Among those proteins the so-called Type IV Coupling Protein plays a central role in the pr

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Deletion of a single helix from the transmembrane domain causes large changes in membrane insertion properties and secondary structure of the bacterial conjugation protein TrwB

Autor: Igor de la Arada, Rosa L. Segura, Ana J. Vecino, Félix M. Goñi, Itziar Alkorta, José Luis R. Arrondo, Fernando de la Cruz

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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TrwB is an essential protein in the conjugative transfer of plasmid R388. The protein consists of a bulky cytosolic domain containing the catalytic site, and a small transmembrane domain (TMD). Our previous studies support the idea that the TMD plays

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Membrane insertion stabilizes the structure of TrwB, the R388 conjugative plasmid coupling protein

Autor: Ana J. Vecino, Igor de la Arada, Félix M. Goñi, Itziar Alkorta, José Luis R. Arrondo, Fernando de la Cruz, Rosa L. Segura

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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TrwB is an integral membrane protein that plays a crucial role in the conjugative process of plasmid R388. We have recently shown [Vecino et al., Biochim. Biophys. Acta 1798(11), 2160-2169 (2010)] that TrwB can be reconstituted into liposomes, and th

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Reconstitution in liposome bilayers enhances nucleotide binding affinity and ATP-specificity of TrwB conjugative coupling protein

Autor: Begoña Ugarte-Uribe, Itsaso Hormaeche, Itziar Alkorta, Félix M. Goñi, Rosa L. Segura, Ana J. Vecino, Fernando de la Cruz, Sandra Águila

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
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Bacterial conjugative systems code for an essential membrane protein that couples the relaxosome to the DNA transport apparatus, called type IV couplingprotein (T4CP). TrwB is the T4CP of the conjugative plasmid R388. In earlier work we found that th

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Purification, Immobilization, and Stabilization of a Lipase from Bacillus thermocatenulatus by Interfacial Adsorption on Hydrophobic Supports

Autor: Jose M. Palomo, María L. Rúa, María A. Pernas, Roberto Fernandez-Lafuente, Gloria Fernández-Lorente, Rosa L. Segura, Jose M. Guisan

Publikováno v: Biotechnology Progress. 20:630-635

A lipase from Bacillus thermocatenulatus (BTL2) cloned in E. coli has been purified using a very simple method: interfacial activation on a hydrophobic support followed by desorption with Triton. Only one band was detected by SDS-PAGE. The pure enzym

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https://doi.org/10.1021/bp0342957

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Glutaraldehyde modification of lipases adsorbed on aminated supports: A simple way to improve their behaviour as enantioselective biocatalyst

Autor: Jose M. Guisan, Roberto Fernandez-Lafuente, Jose M. Palomo, Rosa L. Segura, Gloria Fernández-Lorente

Publikováno v: Enzyme and Microbial Technology. 40:704-707

A new lipase from porcine pancreas was adsorbed on PEI-coated support and utilized in the resolution of (±)-glycidyl butyrate, reaching a moderate E value of 6. The treatment of the adsorbed lipase with glutaraldehyde permitted to increase this valu

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https://doi.org/10.1016/j.enzmictec.2006.05.026

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Purification and identification of different lipases contained in PPL commercial extracts: A minor contaminant is the main responsible of most esterasic activity

Autor: Marco Terreni, Rosa L. Segura, Aurelio Hidalgo, Jose M. Palomo, Roberto Fernandez-Lafuente, Jose M. Guisan, Gloria Fernández-Lorente, Antonio Cortés, Lorena Betancor, Cesar Mateo

Publikováno v: Enzyme and Microbial Technology. 39:817-823

Porcine pancreatic lipase extract has been used as a biocatalyst for many years, however it is a rather complex mixture with various active enzymes. In this work, we have developed a protocol to purify three different enzymes with esterase activity a

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https://doi.org/10.1016/j.enzmictec.2006.01.007

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Unusual enzymatic resolution of (±)-glycidyl-butyrate for the production of (S)-glycidyl derivatives

Autor: Manuel Fuentes, Jose M. Guisan, Jose M. Palomo, Rosa L. Segura, Claudia Ortiz, Roberto Fernandez-Lafuente

Publikováno v: Enzyme and Microbial Technology. 38:429-435

The enzymatic hydrolytic resolution of (±)-glycidyl butyrate using a lipase from Candida antarctica (fraction B) (CAL-B) has been performed. This enzyme presented a significant enantioselectivity towards the R isomer, in contrast with the enantiopre

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https://doi.org/10.1016/j.enzmictec.2005.06.020

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Recent Advances in the Industrial Enzymatic Synthesis of Semi-Synthetic βLactam Antibiotics

Autor: Cesar Mateo, Rober Fernandez-Lafuente, Manuel Fuentes, Rodrigo Torres, Gloria Fernández-Lorente, Jose M. Guisan, Fernando López-Gallego, Rosa L. Segura, Tamara Montes, José Palomo, Valeria Grazú, Lorena Wilson, Olga Abian

Publikováno v: Medicinal Chemistry Reviews - Online. 2:207-218

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https://doi.org/10.2174/1567203054065691

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Synthesis of enantiomerically pure glycidol via a fully enantioselective lipase-catalyzed resolution

Autor: Roberto Fernandez-Lafuente, Jose M. Palomo, Cesar Mateo, Rosa L. Segura, Marco Terreni, Jose M. Guisan

Publikováno v: Tetrahedron: Asymmetry. 16:869-874

The efficient enzymatic synthesis of enantiopure 2,3-epoxypropanol (glycidol) has been achieved. The racemic glycidyl butyrate was successfully resolved by enzymatic hydrolysis using a strategy that combines different immobilization protocols and dif

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https://doi.org/10.1016/j.tetasy.2004.12.027

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