Author/Authors
Dagang Guo، نويسنده , , Burton E. Tropp، نويسنده ,
DocumentNumber
1601550
Title Of Article
A second Escherichia coli protein with CL synthase activity
شماره ركورد
12076
Latin 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.
From Page
263
NaturalLanguageKeyword
Cardiolipin , cls , f413 , N-Terminal deletion , Cardiolipin synthase
JournalTitle
Studia Iranica
To Page
274
To Page
274
Link To Document