The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Editor

Share

Personal info

View

Links

  • Homologues
  • NCBI Gene
  • NCBI SNP
  • iHOP resource
  • OMIM
  • SNPedia
  • UniProt
  • Ensembl
  • HGNC

Table of contents

About

Terms

 

Gene Review: 

GAL3ST3  -  galactose-3-O-sulfotransferase 3

Homo sapiens

Synonyms: Beta-galactose-3-O-sulfotransferase 3, GAL3ST-3, GAL3ST2, Gal-beta-1, 3-GalNAc 3'-sulfotransferase 3, Gal3ST-3, ...
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

High impact information on GAL3ST3

  • Mg(2+), Mn(2+), and Ca(2+) stimulated the activities of Gal3ST-2, whereas only Mg(2+) augmented Gal3ST-3 activity [1].
  • The newly isolated cDNA encodes a novel 3-O-sulfotransferase, termed Gal3ST-3, that acts exclusively on N-acetyllactosamine present in N-glycans and core2-branched O-glycans [2].
  • Moreover, Gal3ST-3 but not Gal3ST-2 can act on Galbeta1-->4(sulfo-->6)GlcNAc, indicating that disulfated sulfo-->3Galbeta1-->4(sulfo-->6) GlcNAc-->R may be formed by Gal3ST-3 in combination with GlcNAc 6-O-sulfotransferase [2].
  • Northern blot analysis demonstrated that transcripts for Gal3ST-3 are predominantly expressed in the brain, kidney, and thyroid where the presence of 3'-sulfation of N-acetyllactosamine has been reported [2].
  • The amino acid sequence of Gal3ST-4 revealed 33%, 39%, and 30% identity to human Gal3ST-1, Gal beta 1-->3/4GlcNAc:-->3'-sulfotransferase (Gal3ST-2) and Gal beta 1-->4GlcNAc:-->3'-sulfotransferase (Gal3ST-3), respectively [3].

References

  1. Identification of physiologically relevant substrates for cloned Gal: 3-O-sulfotransferases (Gal3STs): distinct high affinity of Gal3ST-2 and LS180 sulfotransferase for the globo H backbone, Gal3ST-3 for N-glycan multiterminal Galbeta1, 4GlcNAcbeta units and 6-sulfoGalbeta1, 4GlcNAcbeta, and Gal3ST-4 for the mucin core-2 trisaccharide. Chandrasekaran, E.V., Lakhaman, S.S., Chawda, R., Piskorz, C.F., Neelamegham, S., Matta, K.L. J. Biol. Chem. (2004) [Pubmed]
  2. Molecular cloning and expression of a novel human beta-Gal-3-O-sulfotransferase that acts preferentially on N-acetyllactosamine in N- and O-glycans. Suzuki, A., Hiraoka, N., Suzuki, M., Angata, K., Misra, A.K., McAuliffe, J., Hindsgaul, O., Fukuda, M. J. Biol. Chem. (2001) [Pubmed]
  3. Molecular cloning and characterization of a novel human galactose 3-O-sulfotransferase that transfers sulfate to gal beta 1-->3galNAc residue in O-glycans. Seko, A., Hara-Kuge, S., Yamashita, K. J. Biol. Chem. (2001) [Pubmed]
Contributions to this collaborative article are from individual authors of WikiGenes or mined by the WikiGenes Data Mining Engine from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
 
WikiGenes - Universities