Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
26
pubmed:dateCreated
2006-6-28
pubmed:databankReference
pubmed:abstractText
Elimination of nonnutritional and insoluble compounds is a critical task for any living organism. Flavin-containing monooxygenases (FMOs) attach an oxygen atom to the insoluble nucleophilic compounds to increase solubility and thereby increase excretion. Here we analyze the functional mechanism of FMO from Schizosaccharomyces pombe using the crystal structures of the wild type and protein-cofactor and protein-substrate complexes. The structure of the wild-type FMO revealed that the prosthetic group FAD is an integral part of the protein. FMO needs NADPH as a cofactor in addition to the prosthetic group for its catalytic activity. Structures of the protein-cofactor and protein-substrate complexes provide insights into mechanism of action. We propose that FMOs exist in the cell as a complex with a reduced form of the prosthetic group and NADPH cofactor, readying them to act on substrates. The 4alpha-hydroperoxyflavin form of the prosthetic group represents a transient intermediate of the monooxygenation process. The oxygenated and reduced forms of the prosthetic group help stabilize interactions with cofactor and substrate alternately to permit continuous enzyme turnover.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-10089316, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-10331874, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-10576737, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-10698731, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-10964570, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-11092928, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-11465082, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-11859360, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-11997015, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-12527699, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-12586937, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-12821131, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-1325638, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-15203093, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-15299724, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-15328411, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-16552139, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-1942054, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-2025413, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-36396, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-6087744, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-7984417, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-8377180, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-8954574, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-9254694, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-9536088, http://linkedlifedata.com/resource/pubmed/commentcorrection/16777962-9757107
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9832-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Mechanism of action of a flavin-containing monooxygenase.
pubmed:affiliation
Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural