INVESTIGADORES
BUSI Maria Victoria
artículos
Título:
Polysaccharide-synthesizing Glycosyltransferases and Carbohydrate Binding Modules: the case of Starch Synthase III.
Autor/es:
GOMEZ CASATI, DIEGO; MARTÍN MARIANA; BUSI MARIA VICTORIA
Revista:
PROTEIN AND PEPTIDE LETTERS
Editorial:
BENTHAM SCIENCE PUBL LTD
Referencias:
Lugar: Oak Park; Año: 2013 vol. 20 p. 856 - 863
ISSN:
0929-8665
Resumen:
Glycosyltransferases (GTs) are a ubiquitous group of enzymes that
catalyze the transfer of sugar moieties from activated donor molecules
to specific acceptor molecules, forming glycosidic bonds.
Nucleotide-sugars, lipid phosphate sugars and phosphate sugars can act
as activated donor molecules while acceptor substrates involve
carbohydrates, proteins, lipids, DNA and also, numerous small molecules
(i. e. antibiotics, flavonols, steroids). GTs enzyme families are very
ancient. They are founded in all the three domains of life and display
three different folds (named GT-A, GTB and GT-C) which are a variant of a
common α/β scaffold. In addition, several GTs contain an associated
non-catalytic carbohydrate binding module (CBM) that could be critical
for enzyme activity. This work reviews the current knowledge on the GTs
structures and functions and highlights those enzymes that contain CBMs,
particularly starch binding domains (SBDs). In addition, we also focus
on A. thaliana starch synthase III enzyme, from the GT-5 family. This
protein has a GT-B fold, and contains in its N-terminal region three in
tandem SBDs, which are essential for the regulation of enzyme activity.