PMID:782527
| Citation |
Leppik, RA, Young, IG and Gibson, F (1976) Membrane-associated reactions in ubiquinone biosynthesis in Escherichia coli. 3-Octaprenyl-4-hydroxybenzoate carboxy-lyase. Biochim. Biophys. Acta 436:800-10 |
|---|---|
| Abstract |
A sensitive and quantitative assay for 3-octaprenyl-4-hydroxybenzoate carboxy-lyase has been developed. This enzyme, which catalyses the third reaction in ubiquinone biosynthesis in Escherichia coli, was partially purified and some of its properties determined. It was found that a considerable proportion of the carboxylyase activity could be separated from the membrane fraction in cell extracts prepared using a French press. Gel filtration showed the molecular weight of the enzyme to be about 340 000. For optimal activity the carboxy-lase was shown to require Mn2+, washed membranes or an extract of phospholipids, and an unidentified heat stable factor of molecular weight less than 10 000. The carboxy-lyase reaction was also shown to be strongly stimulated by dithiothreitol and methanol. The properties of the carboxy-lyase are compared with the three other enzymes concerned with ubiquinone biosynthesis in E. coli which have been studied in vitro. The fact that the substrate of the carboxy-lyase is membrane-bound and the enzyme is stimulated by phospholipid suggests that it normally functions in association with the cytoplasmic membrane in vivo. |
| Links | |
| Keywords |
Bacterial Proteins/physiology; Carboxy-Lyases/isolation & purification; Carboxy-Lyases/metabolism; Cations, Divalent/pharmacology; Cell Membrane/enzymology; Dithiothreitol/pharmacology; Enzyme Activation; Escherichia coli/enzymology; Methods; Molecular Weight; Ubiquinone/biosynthesis |
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