Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.3.1.242 extracted from

  • Vorachek-Warren, M.K.; Carty, S.M.; Lin, S.; Cotter, R.J.; Raetz, C.R.
    An Escherichia coli mutant lacking the cold shock-induced palmitoleoyltransferase of lipid A biosynthesis: absence of unsaturated acyl chains and antibiotic hypersensitivity at 12 degrees C (2002), J. Biol. Chem., 277, 14186-14193.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli P0ACV2
-
-

General Information

General Information Comment Organism
malfunction constructed a chromosomal insertion mutation in lpxP, the structural gene for the transferase. Membranes from the lpxP mutant MKV11 grown at 12 °C lack the cold-induced palmitoleoyltransferase present in membranes of cold-shocked wild type cells but retain normal levels of the constitutive lauroyltransferase encoded by lpxL. When examined by mass spectrometry, about two-thirds of the lipid A molecules isolated from wild type Escherichia coli grown at 12 °C contain palmitoleate in place of laurate, whereas the lipid A of cold-adapted mutant MKV11 contain only laurate in amounts comparable with those seen in wild type cells grown at 30°C or above. To probe the integrity of the outer membrane, MKV11 and an isogenic wild type strain are grown at 30 or 12°C and then tested for their susceptibility to antibiotics. MKV11 exhibits a 10fold increase in sensitivity to rifampicin and vancomycin at 12°C compared with wild type cells but shows identical resistance when grown at 30°C. It is suggested that the palmitoleoyltransferase may confer a selective advantage upon Escherichia coli cells growing at lower temperatures by making the outer membrane a more effective barrier to harmful chemicals Escherichia coli