Article
A second Escherichia coli protein with CL synthase activity.
Biochimica et biophysica acta - 17 Jan 2000
Guo D, Tropp B E
Abstract excerpt
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...
Topics
- Cardiolipins
- Cloning, Molecular
- Escherichia coli
- Gene Expression
- Genes, Bacterial
- Kinetics
- Membrane Proteins
- Mutation
- Phospholipase D
- Plasmids
- Temperature
- Transferases (Other Substituted Phosphate Groups)
