10099128

Source:http://linkedlifedata.com/resource/pubmed/id/10099128

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0007382, umls-concept:C0015219, umls-concept:C0562558, umls-concept:C2267219
pubmed:issue	4
pubmed:dateCreated	1999-5-27
pubmed:abstractText	Several contemporary enzymes catalyze alternative reactions distinct from their normal biological reactions. In some cases the alternative reaction is similar to a reaction that is efficiently catalyzed by an evolutionary related enzyme. Alternative activities could have played an important role in the diversification of enzymes by providing a duplicated gene a head start towards being captured by adaptive evolution.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9500160
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Enzymes
pubmed:status	MEDLINE
pubmed:month	Apr
pubmed:issn	1074-5521
pubmed:author	pubmed-author:HerschlagDD, pubmed-author:O'BrienP JPJ
pubmed:issnType	Print
pubmed:volume	6
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	R91-R105
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:10099128-Bacteria, pubmed-meshheading:10099128-Catalysis, pubmed-meshheading:10099128-Enzymes, pubmed-meshheading:10099128-Evolution, Molecular, pubmed-meshheading:10099128-Humans, pubmed-meshheading:10099128-Models, Molecular, pubmed-meshheading:10099128-Protein Engineering
pubmed:year	1999
pubmed:articleTitle	Catalytic promiscuity and the evolution of new enzymatic activities.
pubmed:affiliation	Department of Biochemistry, B400 Beckman Center, Stanford, CA 94305-5307, USA.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't