Biomaterial Database

Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis. 2017

Maria Cecília Zorél Meneghetti, and Tarsis Gesteira Ferreira, and Alexandre Keiji Tashima, and Suely F Chavante, and Edwin Alexander Yates, and Jian Liu, and Helena Bonciani Nader, and Marcelo A Lima

Disciplina de Biologia Molecular, Departamento de Bioquímica, Escola Paulista de Medicina, UNIFESP, São Paulo, Brazil. mlima@unifesp.br.

3-O-Sulfotransferase enzyme (sHS) from Litopenaeus vannamei was cloned and its substrate specificity was investigated against a number of GAG structures, including modified heparin polysaccharides and model oligosaccharides. For the heparin polysaccharides, derived from porcine intestinal mucosa heparin, sulfate groups were incorporated into glucosamine residues containing both N-sulfated and N-acetylated substitution within the regions of the predominant repeating disaccharide, either I-ANS or I-ANAc. However, the resulting polysaccharides did not stabilize antithrombin, which is correlated with anticoagulant activity. It was also shown that the enzyme was able to sulfate disaccharides, I2S-ANS and G-ANAc. The results further illustrate that 3-O-sulfation can be induced outside of the classical heparin-binding pentasaccharide sequence, show that 3-O-sulfation of glucosamine is not a sufficient condition for antithrombin stabilization and suggest that the use of this enzyme during HS biosynthesis may not occur as the final enzymatic step.

UI	MeSH Term	Description	Entries
D008958	Models, Molecular	Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.	Molecular Models,Model, Molecular,Molecular Model
D004795	Enzyme Stability	The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.	Enzyme Stabilities,Stabilities, Enzyme,Stability, Enzyme
D006497	Heparitin Sulfate	A heteropolysaccharide that is similar in structure to HEPARIN. It accumulates in individuals with MUCOPOLYSACCHARIDOSIS.	Heparan Sulfate,Sulfate, Heparan,Sulfate, Heparitin
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia
D013696	Temperature	The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.	Temperatures
D015238	Sulfotransferases	Enzymes which transfer sulfate groups to various acceptor molecules. They are involved in posttranslational sulfation of proteins and sulfate conjugation of exogenous chemicals and bile acids. EC 2.8.2.	Sulfotransferase
D033561	Penaeidae	A family of CRUSTACEA, order DECAPODA, comprising the penaeid shrimp. Species of the genus Penaeus are the most important commercial shrimp throughout the world.	Metapenaeus,Penaeus,Shrimp, Penaeid,Penaeid Shrimp,Penaeid Shrimps,Shrimps, Penaeid