| pubmed-article:15274914 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15274914 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:15274914 | lifeskim:mentions | umls-concept:C0205242 | lld:lifeskim |
| pubmed-article:15274914 | lifeskim:mentions | umls-concept:C0007009 | lld:lifeskim |
| pubmed-article:15274914 | lifeskim:mentions | umls-concept:C0020289 | lld:lifeskim |
| pubmed-article:15274914 | lifeskim:mentions | umls-concept:C0031705 | lld:lifeskim |
| pubmed-article:15274914 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15274914 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:15274914 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:15274914 | pubmed:dateCreated | 2004-7-27 | lld:pubmed |
| pubmed-article:15274914 | pubmed:abstractText | GDP-mannose glycosyl hydrolase (GDPMH) catalyzes the hydrolysis of GDP-mannose and GDP-glucose to GDP and sugar by substitution with inversion at C1 of the sugar. The enzyme has a modified Nudix motif and requires one divalent cation for activity. The 1.3 A X-ray structure of the GDPMH-Mg(2+)-GDP complex, together with kinetic, mutational, and NMR data, suggests a mechanism for the GDPMH reaction. Several residues and the divalent cation strongly promote the departure of the GDP leaving group, supporting a dissociative mechanism. Comparison of the GDPMH structure with that of a typical Nudix hydrolase suggests how sequence changes result in the switch of catalytic activity from P-O bond cleavage to C-O bond cleavage. Changes in the Nudix motif result in loss of binding of at least one Mg(2+) ion, and shortening of a loop by 6 residues shifts the catalytic base by approximately 10 A. | lld:pubmed |
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| pubmed-article:15274914 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15274914 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15274914 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15274914 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15274914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15274914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15274914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15274914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15274914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15274914 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15274914 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15274914 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:15274914 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:15274914 | pubmed:author | pubmed-author:AzurmendiHugo... | lld:pubmed |
| pubmed-article:15274914 | pubmed:author | pubmed-author:MildvanAlbert... | lld:pubmed |
| pubmed-article:15274914 | pubmed:author | pubmed-author:AmzelL... | lld:pubmed |
| pubmed-article:15274914 | pubmed:author | pubmed-author:BianchetMario... | lld:pubmed |
| pubmed-article:15274914 | pubmed:author | pubmed-author:GabelliSandra... | lld:pubmed |
| pubmed-article:15274914 | pubmed:author | pubmed-author:XiaZuyongZ | lld:pubmed |
| pubmed-article:15274914 | pubmed:author | pubmed-author:SarawatVibhor... | lld:pubmed |
| pubmed-article:15274914 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15274914 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:15274914 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15274914 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15274914 | pubmed:pagination | 927-35 | lld:pubmed |
| pubmed-article:15274914 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15274914 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15274914 | pubmed:articleTitle | Structure and mechanism of GDP-mannose glycosyl hydrolase, a Nudix enzyme that cleaves at carbon instead of phosphorus. | lld:pubmed |
| pubmed-article:15274914 | pubmed:affiliation | Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA. | lld:pubmed |
| pubmed-article:15274914 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15274914 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| entrez-gene:946559 | entrezgene:pubmed | pubmed-article:15274914 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:15274914 | lld:pubmed |
