| pubmed-article:19780555 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19780555 | lifeskim:mentions | umls-concept:C0220781 | lld:lifeskim |
| pubmed-article:19780555 | lifeskim:mentions | umls-concept:C1157092 | lld:lifeskim |
| pubmed-article:19780555 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:19780555 | lifeskim:mentions | umls-concept:C0527825 | lld:lifeskim |
| pubmed-article:19780555 | pubmed:issue | 41 | lld:pubmed |
| pubmed-article:19780555 | pubmed:dateCreated | 2009-10-14 | lld:pubmed |
| pubmed-article:19780555 | pubmed:abstractText | Previous studies of the biosynthetic enzymes involved in the assembly of scytonemin (1), a cyanobacterial sunscreen, have identified beta-ketoacid 2 as an important intermediate that is produced by ThDP-dependent enzyme ScyA. We now report that ScyC, previously annotated as a hypothetical protein, catalyzes cyclization and decarboxylation of 2 to generate ketone 5. Assembly of the cyclopentyl[b]indole structure in this manner has little precedent in the chemical literature. Additional mechanistic experiments have revealed that cyclization likely precedes decarboxylation and that the latter event may provide a driving force for cyclopentane formation. | lld:pubmed |
| pubmed-article:19780555 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19780555 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19780555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19780555 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19780555 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:19780555 | pubmed:issn | 1520-5126 | lld:pubmed |
| pubmed-article:19780555 | pubmed:author | pubmed-author:WalshChristop... | lld:pubmed |
| pubmed-article:19780555 | pubmed:author | pubmed-author:BalskusEmily... | lld:pubmed |
| pubmed-article:19780555 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19780555 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:19780555 | pubmed:volume | 131 | lld:pubmed |
| pubmed-article:19780555 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19780555 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19780555 | pubmed:pagination | 14648-9 | lld:pubmed |
| pubmed-article:19780555 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:19780555 | pubmed:meshHeading | pubmed-meshheading:19780555... | lld:pubmed |
| pubmed-article:19780555 | pubmed:meshHeading | pubmed-meshheading:19780555... | lld:pubmed |
| pubmed-article:19780555 | pubmed:meshHeading | pubmed-meshheading:19780555... | lld:pubmed |
| pubmed-article:19780555 | pubmed:meshHeading | pubmed-meshheading:19780555... | lld:pubmed |
| pubmed-article:19780555 | pubmed:meshHeading | pubmed-meshheading:19780555... | lld:pubmed |
| pubmed-article:19780555 | pubmed:meshHeading | pubmed-meshheading:19780555... | lld:pubmed |
| pubmed-article:19780555 | pubmed:meshHeading | pubmed-meshheading:19780555... | lld:pubmed |
| pubmed-article:19780555 | pubmed:meshHeading | pubmed-meshheading:19780555... | lld:pubmed |
| pubmed-article:19780555 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19780555 | pubmed:articleTitle | An enzymatic cyclopentyl[b]indole formation involved in scytonemin biosynthesis. | lld:pubmed |
| pubmed-article:19780555 | pubmed:affiliation | Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
| pubmed-article:19780555 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19780555 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:19780555 | lld:pubmed |
