| pubmed-article:10849007 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10849007 | lifeskim:mentions | umls-concept:C0315079 | lld:lifeskim |
| pubmed-article:10849007 | lifeskim:mentions | umls-concept:C0011175 | lld:lifeskim |
| pubmed-article:10849007 | lifeskim:mentions | umls-concept:C0008801 | lld:lifeskim |
| pubmed-article:10849007 | lifeskim:mentions | umls-concept:C0009226 | lld:lifeskim |
| pubmed-article:10849007 | lifeskim:mentions | umls-concept:C0014898 | lld:lifeskim |
| pubmed-article:10849007 | lifeskim:mentions | umls-concept:C0095920 | lld:lifeskim |
| pubmed-article:10849007 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:10849007 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:10849007 | pubmed:dateCreated | 2000-8-17 | lld:pubmed |
| pubmed-article:10849007 | pubmed:abstractText | Phenyllactate dehydratase from Clostridium sporogenes grown anaerobically on L-phenylalanine catalyses the reversible syn-dehydration of (R)-phenyllactate to (E)-cinnamate. Purification yielded a heterotrimeric enzyme complex (130 +/- 15 kDa) composed of FldA (46 kDa), FldB (43 kDa) and FldC (40 kDa). By re-chromatography on Q-Sepharose, the major part of FldA could be separated and identified as oxygen insensitive cinnamoyl-CoA:phenyllactate CoA-transferase, whereas the transferase depleted trimeric complex retained oxygen sensitive phenyllactate dehydratase activity and contained about one [4Fe-4S] cluster. The dehydratase activity required 10 microM FAD, 0.4 mM ATP, 2.5 mM MgCl2, 0.1 mM NADH, 5 microM cinnamoyl-CoA and small amounts of cell-free extract (10 microg protein per mL) similar to that known for 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. The N-terminus of the homogenous FldA (39 amino acids) is homologous to that of CaiB (39% sequence identity) involved in carnitine metabolism in Escherichia coli. Both enzymes are members of an emerging group of CoA-transferases which exhibit high substrate specificity but apparently do not form enzyme CoA-ester intermediates. It is concluded that dehydration of (R)-phenyllactate to (E)-cinnamate proceeds in two steps, a CoA-transfer from cinnamoyl-CoA to phenyllactate, catalysed by FldA, followed by the dehydration of phenyllactyl-CoA, catalysed by FldB and FldC, whereby the noncovalently bound prosthetic group cinnamoyl-CoA is regenerated. This demonstrates the necessity of a 2-hydroxyacyl-CoA intermediate in the dehydration of 2-hydroxyacids. The transient CoA-ester formation during the dehydration of phenyllactate resembles that during citrate cleavage catalysed by bacterial citrate lyase, which contain a derivative of acetyl-CoA covalently bound to an acyl-carrier-protein (ACP). | lld:pubmed |
| pubmed-article:10849007 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:10849007 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10849007 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10849007 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10849007 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:10849007 | pubmed:author | pubmed-author:LinderDD | lld:pubmed |
| pubmed-article:10849007 | pubmed:author | pubmed-author:BuckelWW | lld:pubmed |
| pubmed-article:10849007 | pubmed:author | pubmed-author:PierikA JAJ | lld:pubmed |
| pubmed-article:10849007 | pubmed:author | pubmed-author:DickertSS | lld:pubmed |
| pubmed-article:10849007 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10849007 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:10849007 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10849007 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10849007 | pubmed:pagination | 3874-84 | lld:pubmed |
| pubmed-article:10849007 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
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| pubmed-article:10849007 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10849007 | pubmed:articleTitle | The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes. | lld:pubmed |
| pubmed-article:10849007 | pubmed:affiliation | Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, Marburg, Germany. | lld:pubmed |
| pubmed-article:10849007 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10849007 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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