Literature summary for 2.8.2.23 extracted from

Meneghetti, M.C.Z.; Gesteira Ferreira, T.; Tashima, A.K.; Chavante, S.F.; Yates, E.A.; Liu, J.; Nader, H.B.; Lima, M.A.
Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis (2017), Org. Biomol. Chem., 15, 6792-6799 .

Search for more literature for 2.8.2.23

Cloned(Commentary)

Cloned (Comment)	Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning of enzyme sHS, and recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 pLysS	Penaeus vannamei

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Penaeus vannamei
Mn2+	required	Penaeus vannamei

Organism

Organism	UniProt	Comment	Textmining
Penaeus vannamei	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 pLysS	Penaeus vannamei

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	substrate specificity analysis, overview. For the heparin polysaccharides, derived from porcine intestinal mucosa heparin, sulfate groups are 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. But the resulting polysaccharides do not stabilize antithrombin, which is correlated with anticoagulant activity. The enzyme is able to sulfate disaccharides, I2S-ANS and G-ANAc. 3-O-sulfation can be induced outside of the classical heparin-binding pentasaccharide sequence. Product analysis by NMR spectroscopy, and antithrombin stabilization analysis by differential scanning fluorimetry (DSF). Only chemically modified heparins served as substrates for sHs whereas chondroitin 4-sulfate, chondroitin 6-sulfate, dermatan sulfate and hyaluronic acid do not. Also N-desulfated-N-reacetylated heparin is not modified by sHS. Acceptor substrates are HS, heparin (Hep), modified heparin: O,N-desuIfated-N-reacetylated (HepNAc), and O,N-desuIfated-N-resuIfated (HepNSuIfo). Enzyme sHS does not require either 2-O-, 6-O- or N-sulfate in heparin/HS to modify the polymer and, N-acetylation does not block 3-O-sulfation as anticipated by the hierarchical biosynthetic process where 3-O-sulfation would happen as the final modification step. The data shows that 3-O-sulfation can occur in distinct biosynthetic steps either being the last HS sulfotransferase in the biosynthesis process or the first one in a non-hierarchical way, according to the oligosaccharides tested	Penaeus vannamei	?	-	-

Synonyms

Synonyms	Comment	Organism
3-O-sulfotransferase	-	Penaeus vannamei
SHS	-	Penaeus vannamei

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Penaeus vannamei

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
100	-	purified recombinant enzyme, 1 min, pH 7.0, inactivation	Penaeus vannamei

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	-	assay at	Penaeus vannamei

General Information

General Information	Comment	Organism
evolution	significant structural similarity between sHs and the human heparan sulfate 3-O-suIfotransferase isoform 5, phylogenetic analysis. The enzyme from Litopenaeus vannamei belongs to the O-sulfotransferase family	Penaeus vannamei
metabolism	role of 3-O-sulfotransferase in heparan sulfate biosynthesis. 3-O-sulfation can occur in distinct biosynthetic steps either being the last HS sulfotransferase in the biosynthesis process or the first one in a non-hierarchical way, according to the oligosaccharides tested	Penaeus vannamei
physiological function	role of 3-O-sulfotransferase in heparan sulfate biosynthesis. 3-O-sulfation can be induced outside of the classical heparin-binding pentasaccharide sequence, and 3-O-sulfation of glucosamine is not a sufficient condition for antithrombin stabilization and suggest that the use of this enzyme during haparan sulfate (HS) biosynthesis may not occur as the final enzymatic step. Thermostabilizing effects of sHS-treated heparins on antithrombin	Penaeus vannamei

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Release 2023.1 (January 2023)