16488653

Source:http://linkedlifedata.com/resource/pubmed/id/16488653

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0005576, umls-concept:C0332185, umls-concept:C0725066
pubmed:issue	2
pubmed:dateCreated	2006-3-29
pubmed:abstractText	Oxygenases continue to be widely studied for selective biooxidation of organic compounds. Protein engineering has resulted in heme and flavin monooxygenases with widely altered substrate specificities, and attempts have been reported to scale-up reactions catalyzed by these enzymes. Cofactor regeneration is still a key issue in these developments. Protein engineering contributed to understanding of structure versus function in dioxygenases.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9811312
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Oxygenases
pubmed:status	MEDLINE
pubmed:month	Apr
pubmed:issn	1367-5931
pubmed:author	pubmed-author:SchmidRolf DRD, pubmed-author:UrlacherVlada BVB
pubmed:issnType	Print
pubmed:volume	10
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	156-61
pubmed:dateRevised	2009-8-25
pubmed:meshHeading	pubmed-meshheading:16488653-Biotransformation, pubmed-meshheading:16488653-Catalysis, pubmed-meshheading:16488653-Oxygenases
pubmed:year	2006
pubmed:articleTitle	Recent advances in oxygenase-catalyzed biotransformations.
pubmed:affiliation	Institute for Technical Biochemistry, University of Stuttgart, Allmandring 31, D-70569 Stuttgart, Germany.
pubmed:publicationType	Journal Article, Review