Source:http://linkedlifedata.com/resource/pubmed/id/10849007
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2000-8-17
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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).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/3-phenyllactic acid,
http://linkedlifedata.com/resource/pubmed/chemical/3-phenylpropionic acid,
http://linkedlifedata.com/resource/pubmed/chemical/Acyl Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Cinnamates,
http://linkedlifedata.com/resource/pubmed/chemical/Coenzyme A,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Esters,
http://linkedlifedata.com/resource/pubmed/chemical/Hydro-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Lactates,
http://linkedlifedata.com/resource/pubmed/chemical/NAD,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylpropionates,
http://linkedlifedata.com/resource/pubmed/chemical/cinnamoyl-coenzyme A
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0014-2956
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
267
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3874-84
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:10849007-Acyl Coenzyme A,
pubmed-meshheading:10849007-Amino Acid Sequence,
pubmed-meshheading:10849007-Cell-Free System,
pubmed-meshheading:10849007-Cinnamates,
pubmed-meshheading:10849007-Clostridium,
pubmed-meshheading:10849007-Coenzyme A,
pubmed-meshheading:10849007-Enzymes,
pubmed-meshheading:10849007-Esters,
pubmed-meshheading:10849007-Fermentation,
pubmed-meshheading:10849007-Hydro-Lyases,
pubmed-meshheading:10849007-Lactates,
pubmed-meshheading:10849007-Molecular Sequence Data,
pubmed-meshheading:10849007-NAD,
pubmed-meshheading:10849007-Operon,
pubmed-meshheading:10849007-Phenylpropionates
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pubmed:year |
2000
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pubmed:articleTitle |
The involvement of coenzyme A esters in the dehydration of (R)-phenyllactate to (E)-cinnamate by Clostridium sporogenes.
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pubmed:affiliation |
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, Marburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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