This chapter presents the specific characteristics of transglutaminases (TGases) in different plant species by comparing them with those of the best-known TGases of animal origin. It, therefore, explains the involvement of TGases in specific aspects of the physiology of plant organisms, highlighting, above all at the cellular level, similar roles, and differences concerning those performed by animal TGases. The features of the putative gene sequences encoding for plant TGases are illustrated with special emphasis on the characteristics of the best-known mammalian TGase 2, among which the presence of the catalytic triad, the binding site for calcium and guanosine triphosphate (GTP), which are present in various plant organisms. The bioinformatics approach has enabled the comparison of the three-dimensional structures of plant TGases with their animal counterparts, suggesting that plant and animal TGases might exhibit a similar three-dimensional conformation from an energetic standpoint. Such similarity holds great significance for catalytic reactions.
Del Duca S., Cai G. (2024). Transglutaminases from plant sources. London : Academic Press [10.1016/B978-0-443-19168-8.00006-7].
Transglutaminases from plant sources
Del Duca S.
Writing – Original Draft Preparation
;
2024
Abstract
This chapter presents the specific characteristics of transglutaminases (TGases) in different plant species by comparing them with those of the best-known TGases of animal origin. It, therefore, explains the involvement of TGases in specific aspects of the physiology of plant organisms, highlighting, above all at the cellular level, similar roles, and differences concerning those performed by animal TGases. The features of the putative gene sequences encoding for plant TGases are illustrated with special emphasis on the characteristics of the best-known mammalian TGase 2, among which the presence of the catalytic triad, the binding site for calcium and guanosine triphosphate (GTP), which are present in various plant organisms. The bioinformatics approach has enabled the comparison of the three-dimensional structures of plant TGases with their animal counterparts, suggesting that plant and animal TGases might exhibit a similar three-dimensional conformation from an energetic standpoint. Such similarity holds great significance for catalytic reactions.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
