Literature summary for 2.7.8.B10 extracted from

Quigley, B.R.; Tropp, B.E.
E. coli cardiolipin synthase: function of N-terminal conserved residues (2009), Biochim. Biophys. Acta, 1788, 2107-2113.

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Protein Variants

Protein Variants	Comment	Organism
delT2-E60	a deletion mutant that is missing residues 260 produces a fully active protein	Escherichia coli
G59A	mutation has little if any effect on cardiolipin synthase processing or activity	Escherichia coli
L7S/V8S	an EYMPE epitope tag is introduced into the interior of Cardiolipin synthase. The tagged polypeptide retains the biological properties of wild type enzyme, including full enzymatic activity. Site-directed mutagenesis is used to alter conserved residues in the N-terminal region. An tagged cardiolipin synthase in which Leu7 and Val8 are both replaced by Ser residues retains in vitro activity but loses most of its in vivo activity. The mutant protein has a higher apparent molecular mass than its parent protein. That conserved residues L7 and V8 play a role in polypeptide processing, topology, or both	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
48000	-	x * 48000, deletion mutant that is missing residues 260, SDS-PAGE	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6H8	-	-

Subunits

Subunits	Comment	Organism
?	x * 48000, deletion mutant that is missing residues 260, SDS-PAGE	Escherichia coli

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Release 2023.1 (January 2023)