Publications by authors named "Barbora Stratilova"
Structural determinants of substrate recognition remain inadequately defined in broad specific cell-wall modifying enzymes, termed xyloglucan xyloglucosyl transferases (XETs). Here, we investigate the Tropaeolum majus seed TmXET6.3 isoform, a member of the GH16_20 subfamily of the GH16 network.
View Article and Find Full Text PDFXyloglucan endotransglycosylases (XETs) play key roles in the remodelling and reconstruction of plant cell walls. These enzymes catalyse homo-transglycosylation reactions with xyloglucan-derived donor and acceptor substrates and hetero-transglycosylation reactions with a variety of structurally diverse polysaccharides. In this work, we describe the basis of acceptor substrate binding specificity in non-specific (TmXET6.
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- Xyloglucan endo-transglycosylases (XETs) are essential enzymes in plants that facilitate cell wall dynamics, influencing growth and adaptation to environmental stress.
- XETs have a unique structure that allows them to catalyze transglycosylation reactions with various xyloglucan-derived donors and acceptors, showcasing their evolutionary diversity.
- The expression of XET genes varies in different plant organs and tissues depending on environmental conditions, highlighting their role in ongoing cell wall restructuring.
Plant xyloglucan xyloglucosyl transferases or xyloglucan endo-transglycosylases (XET; EC 2.4.1.
View Article and Find Full Text PDFWe report on the homo- and hetero-transglycosylation activities of the HvXET3 and HvXET4 xyloglucan xyloglucosyl transferases (XET; EC 2.4.1.
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- Researchers identified the complete primary structure of the Petroselinum crispum protein Pet c 1.0201, which co-purifies with another enzyme and has similarities in molecular mass and isoelectric points.
- The protein belongs to the PR-10 family and is closely related to allergens from celery and carrot, with its details stored in the UniProt Knowledgebase.
- Molecular modeling confirmed its dimeric structure typical of Bet v 1 allergens, but its behavior in salt solutions differed from that of a celery allergen, highlighting distinct dimerization properties.
Article Synopsis
- - Understanding the substrate specificity of Xyloglucan xyloglucosyl transferases (XETs) is crucial for redefining their role in plant cell wall metabolism, challenging the idea that they only interact with cellulose-xyloglucan networks.
- - The study identifies TmXET6.3, an enzyme from Tropaeolum majus, and demonstrates its preference for certain oligosaccharides, outlining key amino acids that influence its substrate interactions.
- - Variants of TmXET6.3 show differing transglycosylation activities, indicating potential for engineering enzymes with enhanced or altered functions in plant cell wall modification.
Characterization of a long-chain α-galactosidase from Papiliotrema flavescens.
World J Microbiol Biotechnol
January 2018
α-Galactosidases are assigned to the class of hydrolases and the subclass of glycoside hydrolases (GHs). They belong to six GH families and include the only characterized α-galactosidases from yeasts (GH 27, Saccharomyces cerevisiae). The present study focuses on an investigation of the lactose-inducible α-galactosidase produced by Papiliotrema flavescens.
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