PMID:368024: Difference between revisions

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<span style = 'font-size: large'> '''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</span>
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!align=left  |Citation
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'''No author listed'''  (1979) Five different enzymatic activities are associated with the multienzyme complex of fatty acid oxidation from Escherichia coli. ''J. Bacteriol.'' '''137''':469-73
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!align=left  |Abstract
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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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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=368024 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC218472 PMC218472]


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|{{TableHeadingColor}} |'''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.
!align=left  |Keywords
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3-Hydroxyacyl CoA Dehydrogenases/metabolism; Acetyl-CoA C-Acyltransferase/metabolism; Electrophoresis, Polyacrylamide Gel; Enoyl-CoA Hydratase; Escherichia coli/enzymology; Fatty Acids/metabolism; Isomerases/metabolism; Multienzyme Complexes/analysis; Multienzyme Complexes/metabolism; Phosphates/pharmacology; Racemases and Epimerases/metabolism; Tromethamine/pharmacology
|{{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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{{LitSignificance}}

Revision as of 19:26, 1 September 2013

Citation

No author listed (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.

Links

PubMed PMC218472

Keywords

3-Hydroxyacyl CoA Dehydrogenases/metabolism; Acetyl-CoA C-Acyltransferase/metabolism; Electrophoresis, Polyacrylamide Gel; Enoyl-CoA Hydratase; Escherichia coli/enzymology; Fatty Acids/metabolism; Isomerases/metabolism; Multienzyme Complexes/analysis; Multienzyme Complexes/metabolism; Phosphates/pharmacology; Racemases and Epimerases/metabolism; Tromethamine/pharmacology

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