Literature DB >> 10634942

A second Escherichia coli protein with CL synthase activity.

D Guo1, B E Tropp.   

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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Year:  2000        PMID： 10634942     DOI： 10.1016/s1388-1981(99)00193-6

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  23 in total

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