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

BRENDA support

Literature summary for 2.4.1.227 extracted from

  • Michaelis, A.M.; Gitai, Z.
    Dynamic polar sequestration of excess MurG may regulate enzymatic function (2010), J. Bacteriol., 192, 4597-4605.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
E268A site-directed mutagenesis, in contrast to wild-type MurG, the MurG lipid interaction mutant often localizes to a single pole Escherichia coli
L79E/F82E site-directed mutagenesis, the mutant does not bind anionic phospholipids but can localize to the cell poles Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane associated Escherichia coli 16020
-
additional information MurG becomes polarly localized when expressed at high cellular concentrations, only at levels that saturate MurGs cellular requirement for growth, the polar MurG is not active Escherichia coli
-
-

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
wild-type strain NCM3722 and diverse modified strains, gene murG
-

Synonyms

Synonyms Comment Organism
MurG
-
Escherichia coli

General Information

General Information Comment Organism
metabolism MurG is an essential N-acetylglucosaminyl transferase involved in catalyzing the final step of peptidoglycan subunit biosynthesis Escherichia coli
additional information MurG becomes polarly localized when expressed at high cellular concentrations, only at levels that saturate MurGs cellular requirement for growth, the polar MurG is not active and polar MurG is dynamic. It can be remobilized when MurG levels drop Escherichia coli
physiological function MurG represents a temporary storage mechanism for excess protein that can later be remobilized into the active pool. Polar MurG can promote polar accumulation of anionic phospholipids Escherichia coli