16221305

Source:http://linkedlifedata.com/resource/pubmed/id/16221305

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0002520, umls-concept:C0025646, umls-concept:C0033809, umls-concept:C0243126, umls-concept:C0733755, umls-concept:C1563389
pubmed:dateCreated	2005-10-27
pubmed:abstractText	The alkaline protease from Pseudomonas aeruginosa (AprA) is a member of the metzincin superfamily of metalloendoproteases. A key feature of these proteases is a conserved methionine-containing 1,4-tight beta turn at the base of the active site zinc binding region.
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101084098
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Methionine, http://linkedlifedata.com/resource/pubmed/chemical/alkaline protease
pubmed:status	MEDLINE
pubmed:issn	1471-2091
pubmed:author	pubmed-author:HonekJohn FJF, pubmed-author:WalasekPaulaP
pubmed:issnType	Electronic
pubmed:volume	6
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	21
pubmed:dateRevised	2010-9-20
pubmed:meshHeading	pubmed-meshheading:16221305-Amino Acid Substitution, pubmed-meshheading:16221305-Bacterial Proteins, pubmed-meshheading:16221305-Binding Sites, pubmed-meshheading:16221305-Endopeptidases, pubmed-meshheading:16221305-Metalloendopeptidases, pubmed-meshheading:16221305-Methionine, pubmed-meshheading:16221305-Protein Structure, Secondary, pubmed-meshheading:16221305-Pseudomonas aeruginosa
pubmed:year	2005
pubmed:articleTitle	Nonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease.
pubmed:affiliation	Department of Chemistry, University of Waterloo, 200 University Avenue, Waterloo, Ontario, Canada N2L 3G1. pwalasek@scimail.uwaterloo.ca
pubmed:publicationType	Journal Article, Comparative Study, Research Support, Non-U.S. Gov't