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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2004-8-6
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pubmed:databankReference |
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1383-94
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15296732-Amino Acid Sequence,
pubmed-meshheading:15296732-Catalytic Domain,
pubmed-meshheading:15296732-Crystallography, X-Ray,
pubmed-meshheading:15296732-Escherichia coli,
pubmed-meshheading:15296732-Formycins,
pubmed-meshheading:15296732-Models, Molecular,
pubmed-meshheading:15296732-Molecular Sequence Data,
pubmed-meshheading:15296732-N-Glycosyl Hydrolases,
pubmed-meshheading:15296732-Pentosyltransferases,
pubmed-meshheading:15296732-Phosphates,
pubmed-meshheading:15296732-Ribonucleotides,
pubmed-meshheading:15296732-Ribosemonophosphates,
pubmed-meshheading:15296732-Sequence Homology, Amino Acid
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pubmed:year |
2004
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pubmed:articleTitle |
Structure of Escherichia coli AMP nucleosidase reveals similarity to nucleoside phosphorylases.
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pubmed:affiliation |
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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