| pubmed-article:15296732 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15296732 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:15296732 | lifeskim:mentions | umls-concept:C0133234 | lld:lifeskim |
| pubmed-article:15296732 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:15296732 | lifeskim:mentions | umls-concept:C2348205 | lld:lifeskim |
| pubmed-article:15296732 | lifeskim:mentions | umls-concept:C0051742 | lld:lifeskim |
| pubmed-article:15296732 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:15296732 | pubmed:dateCreated | 2004-8-6 | lld:pubmed |
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| pubmed-article:15296732 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15296732 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15296732 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15296732 | pubmed:abstractText | AMP nucleosidase (AMN) catalyzes the hydrolysis of AMP to form adenine and ribose 5-phosphate. The enzyme is found only in prokaryotes, where it plays a role in purine nucleoside salvage and intracellular AMP level regulation. Enzyme activity is stimulated by ATP and suppressed by phosphate. The structure of unliganded AMN was determined at 2.7 A resolution, and structures of the complexes with either formycin 5'-monophosphate or inorganic phosphate were determined at 2.6 A and 3.0 A resolution, respectively. AMN is a biological homohexamer, and each monomer is composed of two domains: a catalytic domain and a putative regulatory domain. The overall topology of the catalytic domain and some features of the substrate binding site resemble those of the nucleoside phosphorylases, demonstrating that AMN is a new member of the family. The structure of the regulatory domain consists of a long helix and a four-stranded sheet and has a novel topology. | lld:pubmed |
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| pubmed-article:15296732 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15296732 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15296732 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15296732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15296732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15296732 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15296732 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15296732 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15296732 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:15296732 | pubmed:author | pubmed-author:EalickSteven... | lld:pubmed |
| pubmed-article:15296732 | pubmed:author | pubmed-author:ZhangYangY | lld:pubmed |
| pubmed-article:15296732 | pubmed:author | pubmed-author:CottetSarah... | lld:pubmed |
| pubmed-article:15296732 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15296732 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:15296732 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15296732 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15296732 | pubmed:pagination | 1383-94 | lld:pubmed |
| pubmed-article:15296732 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15296732 | pubmed:meshHeading | pubmed-meshheading:15296732... | lld:pubmed |
| pubmed-article:15296732 | pubmed:meshHeading | pubmed-meshheading:15296732... | lld:pubmed |
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| pubmed-article:15296732 | pubmed:meshHeading | pubmed-meshheading:15296732... | lld:pubmed |
| pubmed-article:15296732 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15296732 | pubmed:articleTitle | Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases. | lld:pubmed |
| pubmed-article:15296732 | pubmed:affiliation | Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA. | lld:pubmed |
| pubmed-article:15296732 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15296732 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15296732 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:946508 | entrezgene:pubmed | pubmed-article:15296732 | lld:entrezgene |
| family:PF10423.4 | family:pubmed | pubmed-article:15296732 | lld:pfam |
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