| Cytidine triphosphate: phosphatidic acid cytidyltransferase in Escherichia coli. | |
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MedLine Citation:
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PMID: 4879388 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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An enzyme has been found in particulate fractions of Escherichia coli that catalyzes the incorporation of cytidine triphosphate (CTP) into lipid in the presence of exogenous phosphatidic acid and Mg(++). The product has been identified enzymatically and by chromatography as cytidine diphosphate diglyceride. The reaction is optimal at a pH of 6.5 and Mg(++) concentration of 5-10 mm. The apparent K(m) for CTP is 7 x 10(-4)M and for phosphatidic acid, 2 x 10(-3)M. The reaction rate falls off rapidly with time and ceases entirely after 1 hr as the result of inactivation of the system by Mg(++). |
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Authors:
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J R Carter |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Journal of lipid research Volume: 9 ISSN: 0022-2275 ISO Abbreviation: J. Lipid Res. Publication Date: 1968 Nov |
Date Detail:
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Created Date: 1968-12-09 Completed Date: 1968-12-09 Revised Date: 2009-10-27 |
Medline Journal Info:
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Nlm Unique ID: 0376606 Medline TA: J Lipid Res Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 748-54 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Cytosine Nucleotides
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metabolism Escherichia coli / enzymology* Glycerides / biosynthesis Hydrogen-Ion Concentration Kinetics Lipids / biosynthesis Magnesium Nucleotidyltransferases / metabolism* Phospholipids Tritium Vibration |
| Chemical | |
Reg. No./Substance:
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0/Cytosine Nucleotides; 0/Glycerides; 0/Lipids; 0/Phospholipids; 10028-17-8/Tritium; 7439-95-4/Magnesium; EC 2.7.7.-/Nucleotidyltransferases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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