21513522

Source:http://linkedlifedata.com/resource/pubmed/id/21513522

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0038172, umls-concept:C0233820, umls-concept:C0243102, umls-concept:C0444626, umls-concept:C1150859, umls-concept:C1517378
pubmed:dateCreated	2011-5-19
pubmed:abstractText	MenH (2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase) is a key enzyme in the biosynthesis of menaquinone, catalyzing an unusual 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate.
pubmed:grant	http://linkedlifedata.com/resource/pubmed/grant/BBS/B/14434, http://linkedlifedata.com/resource/pubmed/grant/WT082596
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-10368274, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-10404588, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-10607665, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-11153266, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-12732651, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-1409539, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-1459959, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-15034147, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-15299313, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-15663942, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-1629162, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-17252134, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-17275835, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-17452350, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-17526854, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-17681537, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-17760421, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-18284213, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-18374194, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-18801996, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-18983854, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-19321747, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-19545176, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-19880382, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-20170126, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-20600129, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-20693690, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-9041628, http://linkedlifedata.com/resource/pubmed/commentcorrection/21513522-9695945
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101088689
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Histidine, http://linkedlifedata.com/resource/pubmed/chemical/Protons, http://linkedlifedata.com/resource/pubmed/chemical/Pyruvic Acid
pubmed:status	MEDLINE
pubmed:issn	1472-6807
pubmed:author	pubmed-author:DawsonAliceA, pubmed-author:FyfePaul KPK, pubmed-author:GilletFlorianF, pubmed-author:HunterWilliam NWN
pubmed:issnType	Electronic
pubmed:volume	11
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	19
pubmed:meshHeading	pubmed-meshheading:21513522-Amino Acid Sequence, pubmed-meshheading:21513522-Bacterial Proteins, pubmed-meshheading:21513522-Biocatalysis, pubmed-meshheading:21513522-Catalytic Domain, pubmed-meshheading:21513522-Crystallography, X-Ray, pubmed-meshheading:21513522-Histidine, pubmed-meshheading:21513522-Hydrogen Bonding, pubmed-meshheading:21513522-Hydrophobic and Hydrophilic Interactions, pubmed-meshheading:21513522-Models, Molecular, pubmed-meshheading:21513522-Molecular Sequence Data, pubmed-meshheading:21513522-Protein Structure, Secondary, pubmed-meshheading:21513522-Protons, pubmed-meshheading:21513522-Pyruvic Acid, pubmed-meshheading:21513522-Sequence Alignment, pubmed-meshheading:21513522-Staphylococcus aureus, pubmed-meshheading:21513522-Structural Homology, Protein, pubmed-meshheading:21513522-Substrate Specificity
pubmed:year	2011
pubmed:articleTitle	Exploiting the high-resolution crystal structure of Staphylococcus aureus MenH to gain insight into enzyme activity.
pubmed:affiliation	Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dundee, DD1 5EH, UK.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't