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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1990-8-13
|
| pubmed:abstractText |
beta-Hydroxydecanoyl-[acyl-carrier-protein] dehydrase catalyzes the essential step in the formation of unsaturated fatty acids in Escherichia coli. This reaction was characterized with native C10 acyl-acyl-carrier protein (ACP) structures in both an aqueous phase system and a substrate immobilization assay system. The dehydrase is equally active with E. coli ACP, recombinant ACP-I derived from spinach, or protein A:ACP-I fusion (acyl-thioesters). There were differences among the substrates in terms of the equilibrium product distribution. Both E. coli acyl-ACP and recombinant acyl-ACP-I as cosubstrates with beta-OH 10:0, trans-2 10:1, or cis-3 10:1 yielded about equal amounts (37 mol%) of the two monoenes regardless of the initial substrate. In contrast, the fusion acyl-ACP-I yielded only 17 mol% cis-3 10:1 with 49 mol% trans-2 10:1 present at equilibrium. These equilibrium values for native cis-3 10:1 are higher than those reported previously for the dehydrase using N-acetylcysteamine thioesters as substrates. The Km values for each beta-OH 10:0 ACP substrate were similar to each other and within the range of in vivo concentrations (5-10 microM). Dehydrase reactivity depends more on acyl chain length than ACP structure or origin and is therefore different from other branch point ACP-utilizing enzymes (plant and bacterial) which discriminate according to ACP structure (D. J. Guerra, J. B. Ohlrogge, and M. Frentzen, 1986, Plant Physiol. 82, 448-453).
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0003-9861
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
1
|
| pubmed:volume |
280
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
336-45
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:2195995-Acyl Carrier Protein,
pubmed-meshheading:2195995-Chemical Phenomena,
pubmed-meshheading:2195995-Chemistry,
pubmed-meshheading:2195995-Escherichia coli,
pubmed-meshheading:2195995-Hydro-Lyases,
pubmed-meshheading:2195995-Recombinant Proteins,
pubmed-meshheading:2195995-Substrate Specificity,
pubmed-meshheading:2195995-Vegetables
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Escherichia coli beta-hydroxydecanoyl thioester dehydrase reacts with native C10 acyl-acyl-carrier proteins of plant and bacterial origin.
|
| pubmed:affiliation |
Institute of Biological Chemistry, Washington State University, Pullman 99164-6340.
|
| pubmed:publicationType |
Journal Article
|