- HS3ST1
Heparan sulfate (glucosamine) 3-O-sulfotransferase 1, also known as HS3ST1, is a human
gene .cite web | title = Entrez Gene: HS3ST1 heparan sulfate (glucosamine) 3-O-sulfotransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9957| accessdate = ]PBB_Summary
section_title =
summary_text = Heparan sulfate biosynthetic enzymes are key components in generating a myriad of distinct heparan sulfate fine structures that carry out multiple biologic activities. The enzyme encoded by this gene is a member of the heparan sulfate biosynthetic enzyme family. It possesses both heparan sulfate glucosaminyl 3-O-sulfotransferase activity, anticoagulant heparan sulfate conversion activity, and is a rate limiting enzyme for synthesis of anticoagulant heparan. This enzyme is an intraluminal Golgi resident protein.cite web | title = Entrez Gene: HS3ST1 heparan sulfate (glucosamine) 3-O-sulfotransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9957| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Razi N, Lindahl U |title=Biosynthesis of heparin/heparan sulfate. The D-glucosaminyl 3-O-sulfotransferase reaction: target and inhibitor saccharides. |journal=J. Biol. Chem. |volume=270 |issue= 19 |pages= 11267–75 |year= 1995 |pmid= 7744762 |doi=
*cite journal | author=Liu J, Shworak NW, Fritze LM, "et al." |title=Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. |journal=J. Biol. Chem. |volume=271 |issue= 43 |pages= 27072–82 |year= 1996 |pmid= 8900198 |doi=
*cite journal | author=Shworak NW, Liu J, Fritze LM, "et al." |title=Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase. |journal=J. Biol. Chem. |volume=272 |issue= 44 |pages= 28008–19 |year= 1997 |pmid= 9346953 |doi=
*cite journal | author=Shworak NW, Liu J, Petros LM, "et al." |title=Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci. |journal=J. Biol. Chem. |volume=274 |issue= 8 |pages= 5170–84 |year= 1999 |pmid= 9988767 |doi=
*cite journal | author=Liu J, Shworak NW, Sinaÿ P, "et al." |title=Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities. |journal=J. Biol. Chem. |volume=274 |issue= 8 |pages= 5185–92 |year= 1999 |pmid= 9988768 |doi=
*cite journal | author=Hernaiz M, Liu J, Rosenberg RD, Linhardt RJ |title=Enzymatic modification of heparan sulfate on a biochip promotes its interaction with antithrombin III. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 1 |pages= 292–7 |year= 2000 |pmid= 11006120 |doi= 10.1006/bbrc.2000.3453
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Edavettal SC, Carrick K, Shah RR, "et al." |title=A conformational change in heparan sulfate 3-O-sulfotransferase-1 is induced by binding to heparan sulfate. |journal=Biochemistry |volume=43 |issue= 16 |pages= 4680–8 |year= 2004 |pmid= 15096036 |doi= 10.1021/bi0499112
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504PBB_Controls
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