| pubmed-article:17185228 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17185228 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:17185228 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:17185228 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:17185228 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17185228 | lifeskim:mentions | umls-concept:C2713412 | lld:lifeskim |
| pubmed-article:17185228 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:17185228 | pubmed:dateCreated | 2006-12-22 | lld:pubmed |
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| pubmed-article:17185228 | pubmed:abstractText | Aromatic amino acid ammonia-lyases catalyze the deamination of L-His, L-Phe, and L-Tyr, yielding ammonia plus aryl acids bearing an alpha,beta-unsaturated propenoic acid. We report crystallographic analyses of unliganded Rhodobacter sphaeroides tyrosine ammonia-lyase (RsTAL) and RsTAL bound to p-coumarate and caffeate. His 89 of RsTAL forms a hydrogen bond with the p-hydroxyl moieties of coumarate and caffeate. His 89 is conserved in TALs but replaced in phenylalanine ammonia-lyases (PALs) and histidine ammonia-lyases (HALs). Substitution of His 89 by Phe, a characteristic residue of PALs, yields a mutant with a switch in kinetic preference from L-Tyr to L-Phe. Structures of the H89F mutant in complex with the PAL product, cinnamate, or the PAL-specific inhibitor, 2-aminoindan-2-phosphonate (AIP), support the role of position 89 as a specificity determinant in the family of aromatic amino acid ammonia-lyases and aminomutases responsible for beta-amino acid biosynthesis. | lld:pubmed |
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| pubmed-article:17185228 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17185228 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17185228 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17185228 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17185228 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17185228 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:17185228 | pubmed:issn | 1074-5521 | lld:pubmed |
| pubmed-article:17185228 | pubmed:author | pubmed-author:NoelJoseph... | lld:pubmed |
| pubmed-article:17185228 | pubmed:author | pubmed-author:BowmanMariann... | lld:pubmed |
| pubmed-article:17185228 | pubmed:author | pubmed-author:MooreBradley... | lld:pubmed |
| pubmed-article:17185228 | pubmed:author | pubmed-author:MoffittMichel... | lld:pubmed |
| pubmed-article:17185228 | pubmed:author | pubmed-author:LouieGordon... | lld:pubmed |
| pubmed-article:17185228 | pubmed:author | pubmed-author:BaigaThomas... | lld:pubmed |
| pubmed-article:17185228 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17185228 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:17185228 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17185228 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17185228 | pubmed:pagination | 1327-38 | lld:pubmed |
| pubmed-article:17185228 | pubmed:dateRevised | 2010-12-3 | lld:pubmed |
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| pubmed-article:17185228 | pubmed:meshHeading | pubmed-meshheading:17185228... | lld:pubmed |
| pubmed-article:17185228 | pubmed:meshHeading | pubmed-meshheading:17185228... | lld:pubmed |
| pubmed-article:17185228 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17185228 | pubmed:articleTitle | Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases. | lld:pubmed |
| pubmed-article:17185228 | pubmed:affiliation | Howard Hughes Medical Institute, Jack H. Skirball Center for Chemical Biology and Proteomics, The Salk Institute for Biological Studies, La Jolla, California 92037, USA. | lld:pubmed |
| pubmed-article:17185228 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17185228 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:17185228 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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