PMID:10634942
| Citation |
Guo, D and Tropp, BE (2000) A second Escherichia coli protein with CL synthase activity. Biochim. Biophys. Acta 1483:263-74 |
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| Abstract |
The Escherichia coli open reading frame f413, which has the potential to code for a polypeptide homologous to cardiolipin (CL) synthase, has been cloned. Its polypeptide product has a molecular mass of 48 kDa, is membrane-bound, and catalyzes CL formation but does not hydrolyze CL. A comparison of the sequences predicted for the polypeptides encoded by f413 and cls indicates that the N-terminal residues specified by cls may be unnecessary for CL synthase activity. Construction of a truncated cls gene and characterization of its polypeptide product have confirmed this conclusion. |
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| Keywords |
Cardiolipins/metabolism; Cloning, Molecular; Escherichia coli/enzymology; Escherichia coli/genetics; Gene Expression; Genes, Bacterial; Kinetics; Membrane Proteins; Mutation; Phospholipase D/metabolism; Plasmids; Temperature; Transferases (Other Substituted Phosphate Groups)/chemistry; Transferases (Other Substituted Phosphate Groups)/genetics; Transferases (Other Substituted Phosphate Groups)/metabolism |
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