| pubmed-article:20665018 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20665018 | lifeskim:mentions | umls-concept:C0014279 | lld:lifeskim |
| pubmed-article:20665018 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:20665018 | lifeskim:mentions | umls-concept:C0311400 | lld:lifeskim |
| pubmed-article:20665018 | lifeskim:mentions | umls-concept:C0536390 | lld:lifeskim |
| pubmed-article:20665018 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:20665018 | pubmed:dateCreated | 2010-9-14 | lld:pubmed |
| pubmed-article:20665018 | pubmed:abstractText | The stereo-specific L-isoleucine-4-hydroxylase (L-isoleucine dioxygenase (IDO)) was cloned and expressed in an Escherichia coli 2? strain lacking the activities of ?-ketoglutarate dehydrogenase (EC 1.2.4.2), isocitrate liase (EC 4.1.3.1), and isocitrate dehydrogenase kinase/phosphatase (EC 2.7.11.5). The 2? strain could not grow in a minimal-salt/glucose/glycerol medium due to the blockage of TCA during succinate synthesis. The IDO activity in the 2? strain was able to "shunt" destroyed TCA, thereby coupling L-isoleucine hydroxylation and cell growth. Using this strain, we performed the direct biotransformation of L-isoleucine into 4-HIL with an 82% yield. | lld:pubmed |
| pubmed-article:20665018 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20665018 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20665018 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20665018 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20665018 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20665018 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20665018 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20665018 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20665018 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:20665018 | pubmed:issn | 1432-0614 | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:OgawaJunJ | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:ShimizuSakayu... | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:SmirnovSergey... | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:SamsonovaNata... | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:HibiMakotoM | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:KoderaTomohir... | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:KiveroAlexand... | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:KotlyarovaVer... | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:RushkevichNat... | lld:pubmed |
| pubmed-article:20665018 | pubmed:author | pubmed-author:SokolovPavel... | lld:pubmed |
| pubmed-article:20665018 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20665018 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:20665018 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20665018 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20665018 | pubmed:pagination | 719-26 | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:meshHeading | pubmed-meshheading:20665018... | lld:pubmed |
| pubmed-article:20665018 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20665018 | pubmed:articleTitle | Metabolic engineering of Escherichia coli to produce (2S, 3R, 4S)-4-hydroxyisoleucine. | lld:pubmed |
| pubmed-article:20665018 | pubmed:affiliation | Ajinomoto-Genetika Research Institute, 1st Dorozhny Pr. 1, Moscow 117545, Russia. servasmi@mail.ru | lld:pubmed |
| pubmed-article:20665018 | pubmed:publicationType | Journal Article | lld:pubmed |
