PMID:368024: Difference between revisions
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|{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=368024 PubMed] | |{{TableHeadingColor}} nowrap |'''Links''' || [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=368024 PubMed] | ||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
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==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Revision as of 22:44, 25 April 2008
Pramanik, A, Pawar, S, Antonian, E and Schulz, H (1979) Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli.J. Bacteriol. 137:469-73
| Abstract | The purified multienzyme complex of fatty acid oxidation from Escherichia coli was found to possess 3-hydroxyacyl-coenzyme A (CoA) epimerase and cis-delta3-trans-delta2-enoyl-CoA isomerase activities in addition to the previously identified enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, and 3-ketoactyl-CoA thiolase activities. Evidence is presented in support of the proposed association of all five enzyme activities with one protein which apparently is composed of two types of subunits and which can exist in several aggregated forms. The five component enzymes of the complex were rapidly inactivated by tris(hydroxymethyl)aminomethane, whereas they remained active in the presence of potassium phosphate. |
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