pubmed-article:20533322 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:20533322 | lifeskim:mentions | umls-concept:C0220806 | lld:lifeskim |
pubmed-article:20533322 | lifeskim:mentions | umls-concept:C0996217 | lld:lifeskim |
pubmed-article:20533322 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
pubmed-article:20533322 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
pubmed-article:20533322 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
pubmed-article:20533322 | lifeskim:mentions | umls-concept:C0302523 | lld:lifeskim |
pubmed-article:20533322 | lifeskim:mentions | umls-concept:C0700325 | lld:lifeskim |
pubmed-article:20533322 | lifeskim:mentions | umls-concept:C0037813 | lld:lifeskim |
pubmed-article:20533322 | pubmed:issue | 13 | lld:pubmed |
pubmed-article:20533322 | pubmed:dateCreated | 2010-6-10 | lld:pubmed |
pubmed-article:20533322 | pubmed:abstractText | The direct detection of intermediates in enzymatic reactions can yield important mechanistic insights but may be difficult due to short intermediate lifetimes and chemical instability. Using a rapid-mixing device coupled with electrospray ionization time-of-flight mass spectrometry, the noncovalent hemiketal intermediate in the reaction of metal-dependent 3-deoxy-D-manno-octulosonate-8-phosphate (KDO8P) synthase from Aquifex pyrophilus was observed in the millisecond time range. Using single turnover conditions, the noncovalent complexes of enzyme with Cd(2+):phosphoenolpyruvate, Cd(2+):phosphate, Cd(2+):KDO8P, and Cd(2+):intermediate complexes were resolved. The intermediate complex is present during times ranging from 50-630 ms, indicating that the intermediate builds up at the ambient temperatures of the experiment. This represents the first direct detection of the intermediate with a native metal-dependent KDO8PS, and further demonstrates that time-resolved mass spectrometry is a useful tool in mechanistic studies of enzymatic reactions. | lld:pubmed |
pubmed-article:20533322 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:language | eng | lld:pubmed |
pubmed-article:20533322 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:20533322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:20533322 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:20533322 | pubmed:month | Jul | lld:pubmed |
pubmed-article:20533322 | pubmed:issn | 1097-0231 | lld:pubmed |
pubmed-article:20533322 | pubmed:author | pubmed-author:AndersonKaren... | lld:pubmed |
pubmed-article:20533322 | pubmed:author | pubmed-author:FurduiCristin... | lld:pubmed |
pubmed-article:20533322 | pubmed:author | pubmed-author:RobertsAnneA | lld:pubmed |
pubmed-article:20533322 | pubmed:copyrightInfo | Copyright 2010 John Wiley & Sons, Ltd. | lld:pubmed |
pubmed-article:20533322 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:20533322 | pubmed:day | 15 | lld:pubmed |
pubmed-article:20533322 | pubmed:volume | 24 | lld:pubmed |
pubmed-article:20533322 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:20533322 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:20533322 | pubmed:pagination | 1919-24 | lld:pubmed |
pubmed-article:20533322 | pubmed:dateRevised | 2010-10-1 | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:meshHeading | pubmed-meshheading:20533322... | lld:pubmed |
pubmed-article:20533322 | pubmed:year | 2010 | lld:pubmed |
pubmed-article:20533322 | pubmed:articleTitle | Observation of a chemically labile, noncovalent enzyme intermediate in the reaction of metal-dependent Aquifex pyrophilus KDO8PS by time-resolved mass spectrometry. | lld:pubmed |
pubmed-article:20533322 | pubmed:affiliation | Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06510, USA. | lld:pubmed |
pubmed-article:20533322 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:20533322 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |