Source:http://linkedlifedata.com/resource/pubmed/id/12872993
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2003-7-22
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pubmed:abstractText |
Orotic acid phosphoribosyltransferase (PyrE) (EC 2.4.2.10) is a key enzyme in de novo uridine monophosphate (UMP) biosynthesis. It catalyzes the reaction between orotic acid and 5-phosphoribosyl-1-pyrophosphate (PRPP) to yield orotidine monophosphate (OMP), which is transformed to uridine monophosphate by decarboxylation. H. pylori PyrE was crystallized at 294 +/- 1 K by the hanging drop vapor-diffusion method. The crystals belong to the space group P2(1)2(1)2(1) with unit-cell dimensions a = 95.8, b = 104.9, c = 281.1 A, alpha = beta = gamma = 90 degrees. A set of diffraction data was collected to 3.29 A resolution using synchrotron X-ray radiation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1016-8478
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
361-3
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12872993-Crystallization,
pubmed-meshheading:12872993-Crystallography, X-Ray,
pubmed-meshheading:12872993-Escherichia coli,
pubmed-meshheading:12872993-Helicobacter pylori,
pubmed-meshheading:12872993-Orotate Phosphoribosyltransferase,
pubmed-meshheading:12872993-Protein Conformation,
pubmed-meshheading:12872993-Salmonella typhimurium,
pubmed-meshheading:12872993-Sequence Alignment,
pubmed-meshheading:12872993-Transfection
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pubmed:year |
2003
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pubmed:articleTitle |
Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori.
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pubmed:affiliation |
Department of Life Science, Kwangju Institute of Science and Technology, Gwangju 500-712, Korea.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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