| pubmed-article:17559390 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17559390 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:17559390 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:17559390 | lifeskim:mentions | umls-concept:C0679199 | lld:lifeskim |
| pubmed-article:17559390 | lifeskim:mentions | umls-concept:C1883254 | lld:lifeskim |
| pubmed-article:17559390 | lifeskim:mentions | umls-concept:C1817834 | lld:lifeskim |
| pubmed-article:17559390 | lifeskim:mentions | umls-concept:C0765250 | lld:lifeskim |
| pubmed-article:17559390 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:17559390 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:17559390 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17559390 | pubmed:dateCreated | 2007-7-5 | lld:pubmed |
| pubmed-article:17559390 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:abstractText | A two-step enzymatic synthesis process of 4-hydroxyisoleucine is suggested. In the first step, the aldol condensation of acetaldehyde and alpha-ketobutyrate catalyzed by specific aldolase results in the formation of 4-hydroxy-3-methyl-2-keto-pentanoate (HMKP). In the second step, amination of HMKP by the branched-chain amino acid aminotransferase leads to synthesis of 4-hydroxyisoleucine. An enzyme possessing HMKP aldolase activity (asHPAL) was purified 2500-fold from a crude extract of Arthrobacter simplex strain AKU 626. Sequencing of the asHPAL structural gene showed that the purified enzyme belongs to the HpcH/HpaI aldolase family. The 4-hydroxyisoleucine was synthesized in vitro from acetaldehyde, alpha-ketobutyrate and l-glutamate using a coupled aldolase/branched-chain amino acid aminotransferase bienzymatic reaction. | lld:pubmed |
| pubmed-article:17559390 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17559390 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17559390 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17559390 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:17559390 | pubmed:issn | 0378-1097 | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:OgawaJunJ | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:ShimizuSakayu... | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:SmirnovSergey... | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:YamanakaHiroy... | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:SamsonovaNata... | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:NovikovaAnna... | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:MatrosovNikol... | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:RushkevichNat... | lld:pubmed |
| pubmed-article:17559390 | pubmed:author | pubmed-author:KoderaTomohir... | lld:pubmed |
| pubmed-article:17559390 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17559390 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:17559390 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17559390 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17559390 | pubmed:pagination | 70-7 | lld:pubmed |
| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
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| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
| pubmed-article:17559390 | pubmed:meshHeading | pubmed-meshheading:17559390... | lld:pubmed |
| pubmed-article:17559390 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17559390 | pubmed:articleTitle | A novel strategy for enzymatic synthesis of 4-hydroxyisoleucine: identification of an enzyme possessing HMKP (4-hydroxy-3-methyl-2-keto-pentanoate) aldolase activity. | lld:pubmed |
| pubmed-article:17559390 | pubmed:affiliation | Ajinomoto-Genetika Research Institute, 1st Dorozhny pr. 1, Moscow, Russia. servasmi@rol.ru | lld:pubmed |
| pubmed-article:17559390 | pubmed:publicationType | Journal Article | lld:pubmed |
