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| pubmed-article:10319816 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
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| pubmed-article:10319816 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:10319816 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10319816 | pubmed:dateCreated | 1999-5-20 | lld:pubmed |
| pubmed-article:10319816 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10319816 | pubmed:abstractText | Serotonin N-acetyltransferase, a member of the GNAT acetyltransferase superfamily, is the penultimate enzyme in the conversion of serotonin to melatonin, the circadian neurohormone. Comparison of the structures of the substrate-free enzyme and the complex with a bisubstrate analog, coenzyme A-S-acetyltryptamine, demonstrates that acetyl coenzyme A (AcCoA) binding is accompanied by a large conformational change that in turn leads to the formation of the serotonin-binding site. The structure of the complex also provides insight into how the enzyme may facilitate acetyl transfer. A water-filled channel leading from the active site to the surface provides a pathway for proton removal following amine deprotonation. Furthermore, structural and mutagenesis results indicate an important role for Tyr-168 in catalysis. | lld:pubmed |
| pubmed-article:10319816 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10319816 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10319816 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10319816 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10319816 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:10319816 | pubmed:author | pubmed-author:KleinD CDC | lld:pubmed |
| pubmed-article:10319816 | pubmed:author | pubmed-author:NamboodiriM... | lld:pubmed |
| pubmed-article:10319816 | pubmed:author | pubmed-author:DydaFF | lld:pubmed |
| pubmed-article:10319816 | pubmed:author | pubmed-author:HickmanA BAB | lld:pubmed |
| pubmed-article:10319816 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10319816 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:10319816 | pubmed:volume | 97 | lld:pubmed |
| pubmed-article:10319816 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10319816 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10319816 | pubmed:pagination | 361-9 | lld:pubmed |
| pubmed-article:10319816 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:10319816 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10319816 | pubmed:articleTitle | The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog. | lld:pubmed |
| pubmed-article:10319816 | pubmed:affiliation | Laboratory of Developmental Neurobiology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-0560, USA. | lld:pubmed |
| pubmed-article:10319816 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10319816 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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