Biology:CHST7
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Carbohydrate sulfotransferase 7 is an enzyme that in humans is encoded by the CHST7 gene.[1][2]
Function
This gene belongs to the sulfotransferase gene family. Sulfotransferases generate sulfated glycosaminoglycan (GAG) moieties during chondroitin sulfate biosynthesis. They create considerable structural diversity among chondroitin sulfates by transferring sulfate with remarkable specificity for the underlying oligosaccharide substrate. This gene product mainly transfers sulfate to N-acetylgalactosamine. The regulated expression of each member of this gene family may be an important determinant of sulfated GAGs expression and the associated function of chondroitin sulfates as regulators of many biologic processes. This gene is part of a gene cluster on chromosome Xp11.23.[2]
References
- ↑ "Molecular cloning and expression of a novel chondroitin 6-O-sulfotransferase". J Biol Chem 275 (28): 21075–80. Aug 2000. doi:10.1074/jbc.M002101200. PMID 10781596.
- ↑ 2.0 2.1 "Entrez Gene: CHST7 carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=56548.
External links
- Human CHST7 genome location and CHST7 gene details page in the UCSC Genome Browser.
Further reading
- Liu T; Qian WJ; Gritsenko MA et al. (2006). "Human Plasma N-Glycoproteome Analysis by Immunoaffinity Subtraction, Hydrazide Chemistry, and Mass Spectrometry". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMID 16335952.
- Ross MT; Grafham DV; Coffey AJ et al. (2005). "The DNA sequence of the human X chromosome". Nature 434 (7031): 325–37. doi:10.1038/nature03440. PMID 15772651. Bibcode: 2005Natur.434..325R.
- Gerhard DS; Wagner L; Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
- Strausberg RL; Feingold EA; Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- Thiselton DL; McDowall J; Brandau O et al. (2002). "An integrated, functionally annotated gene map of the DXS8026-ELK1 interval on human Xp11.3-Xp11.23: potential hotspot for neurogenetic disorders". Genomics 79 (4): 560–72. doi:10.1006/geno.2002.6733. PMID 11944989.
- Bhakta S; Bartes A; Bowman KG et al. (2001). "Sulfation of N-acetylglucosamine by chondroitin 6-sulfotransferase 2 (GST-5)". J. Biol. Chem. 275 (51): 40226–34. doi:10.1074/jbc.M006414200. PMID 10956661.
- Uchimura K; Fasakhany F; Kadomatsu K et al. (2000). "Diversity of N-acetylglucosamine-6-O-sulfotransferases: molecular cloning of a novel enzyme with different distribution and specificities". Biochem. Biophys. Res. Commun. 274 (2): 291–6. doi:10.1006/bbrc.2000.3141. PMID 10913333.
- Shilatifard A; Merkle RK; Helland DE et al. (1993). "Complex-type N-linked oligosaccharides of gp120 from human immunodeficiency virus type 1 contain sulfated N-acetylglucosamine". J. Virol. 67 (2): 943–52. doi:10.1128/JVI.67.2.943-952.1993. PMID 8419650.
- "Sulfation of the human immunodeficiency virus envelope glycoprotein". J. Virol. 66 (12): 6953–9. 1992. doi:10.1128/JVI.66.12.6953-6959.1992. PMID 1433500.
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