| pubmed-article:20118238 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20118238 | lifeskim:mentions | umls-concept:C0019143 | lld:lifeskim |
| pubmed-article:20118238 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:20118238 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:20118238 | lifeskim:mentions | umls-concept:C1825366 | lld:lifeskim |
| pubmed-article:20118238 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:20118238 | pubmed:dateCreated | 2010-4-5 | lld:pubmed |
| pubmed-article:20118238 | pubmed:abstractText | Heparan sulfate (HS) is involved in essential physiological and pathophysiological functions. HS is a highly sulfated polysaccharide consisting of glucuronic acid (or iduronic acid) linked to glucosamine carrying various sulfo groups. Biosynthesis of HS involves sulfotransferases and an epimerase. The HS C(5)-epimerase converts glucuronic acid to iduronic acid. The method for determining the activity has been cumbersome due to the use of a site-specifically (3)H-labeled polysaccharide substrate. Here, we report a two-enzyme coupling assay to determine the activity of C(5)-epimerase. HS 2-O-sulfotransferase (2OST) transfers the sulfo group to the 2-OH-position of glucuronic or iduronic acid. Unlike the wild type protein, 2-O-sulfotransferase mutant (2OST Y94I) transfers sulfate to the iduronic acid but not to the glucuronic acid. Thus, 2OST Y94I cannot sulfate N-sulfated heparosan, a polysaccharide containing glucuronic acid. Incubating N-sulfated heparosan with C(5)-epimerase converts some of the glucuronic acid to iduronic acid, thus becoming a substrate for 2OST Y94I. The susceptibility of the C(5)-epimerase-treated N-sulfated heparosan to 2OST Y94I modification directly correlates to the amount of the activity of C(5)-epimerase, proving that this two-enzyme coupling system can be used to assay for C(5)-epimerase. The method was further used to determine the activities of various C(5)-epimerase mutants. Our approach will significantly reduce the complexity for assaying the activity of C(5)-epimerase and facilitate the structural and functional analysis of C(5)-epimerase. | lld:pubmed |
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| pubmed-article:20118238 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20118238 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20118238 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20118238 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20118238 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20118238 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20118238 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20118238 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:20118238 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20118238 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20118238 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:20118238 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20118238 | pubmed:author | pubmed-author:HaM JMJ | lld:pubmed |
| pubmed-article:20118238 | pubmed:author | pubmed-author:LiuJianJ | lld:pubmed |
| pubmed-article:20118238 | pubmed:author | pubmed-author:BetheaHeather... | lld:pubmed |
| pubmed-article:20118238 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20118238 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:20118238 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20118238 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20118238 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20118238 | pubmed:pagination | 11106-13 | lld:pubmed |
| pubmed-article:20118238 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
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| pubmed-article:20118238 | pubmed:meshHeading | pubmed-meshheading:20118238... | lld:pubmed |
| pubmed-article:20118238 | pubmed:meshHeading | pubmed-meshheading:20118238... | lld:pubmed |
| pubmed-article:20118238 | pubmed:meshHeading | pubmed-meshheading:20118238... | lld:pubmed |
| pubmed-article:20118238 | pubmed:meshHeading | pubmed-meshheading:20118238... | lld:pubmed |
| pubmed-article:20118238 | pubmed:meshHeading | pubmed-meshheading:20118238... | lld:pubmed |
| pubmed-article:20118238 | pubmed:meshHeading | pubmed-meshheading:20118238... | lld:pubmed |
| pubmed-article:20118238 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20118238 | pubmed:articleTitle | Using engineered 2-O-sulfotransferase to determine the activity of heparan sulfate C5-epimerase and its mutants. | lld:pubmed |
| pubmed-article:20118238 | pubmed:affiliation | Division of Medicinal Chemistry and Natural Products, Eshelman School of Pharmacy, University of North Carolina, Chapel Hill, North Carolina 27599, USA. | lld:pubmed |
| pubmed-article:20118238 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20118238 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20118238 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:93683 | entrezgene:pubmed | pubmed-article:20118238 | lld:entrezgene |
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