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

BRENDA support

Literature summary extracted from

  • Fuehrer, F.; Langklotz, S.; Narberhaus, F.
    The C-terminal end of LpxC is required for degradation by the FtsH protease (2006), Mol. Microbiol., 59, 1025-1036.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.108 Escherichia coli BL21 is used as host for expression of Strep-tagged LpxC protein Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.4.24.B17 membrane
-
 Escherichia coli 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.1.108 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O Escherichia coli the enzyme is involved in lipid A biosynthesis UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?
3.5.1.108 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O Escherichia coli W3110 / ATCC 27325 the enzyme is involved in lipid A biosynthesis UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.B17 Escherichia coli
-
-
-
3.4.24.B17 Escherichia coli W3110 / ATCC 27325
-
-
-
3.5.1.108 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.24.B17 protein LpxC + H2O protein LpxC is UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase Escherichia coli ?
-
 ?
3.4.24.B17 protein LpxC + H2O protein LpxC is UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase Escherichia coli W3110 / ATCC 27325 ?
-
 ?
3.4.24.B17 protein sigma32 + H2O protein sigma32 is also called RhoP Escherichia coli ?
-
 ?
3.4.24.B17 protein sigma32 + H2O protein sigma32 is also called RhoP Escherichia coli W3110 / ATCC 27325 ?
-
 ?
3.5.1.108 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
-
 Escherichia coli UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?
3.5.1.108 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O the enzyme is involved in lipid A biosynthesis Escherichia coli UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?
3.5.1.108 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
-
 Escherichia coli W3110 / ATCC 27325 UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?
3.5.1.108 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O the enzyme is involved in lipid A biosynthesis Escherichia coli W3110 / ATCC 27325 UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.24.B17 FtsH
-
 Escherichia coli
3.5.1.108 LpxC protein
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
3.5.1.108 physiological function the viability of Gram negative bacteria depends on lipid A, which is the anchoring component of lipopolysaccharides in the outer membrane. Lipopolysaccharides provides a permeability barrier to the cell and Escherichia coli mutants affected in lipopolysaccharide biosynthesis are hypersensitive to antibiotics and detergents. Lipid A is the immuno-effective portion of lipopolysaccharide causing a septic shock by Gram negative bacteria. Lipid A and the enzymes involved in lipopolysaccharide biosynthesis are considered to be attractive drug targets. Although LPS is essential, Escherichia coli is unable to tolerate elevated levels of it, which induces accumulation of abnormal membranes. The proper lipopolysaccharide amount depends on the cellular level of the UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase LpxC, the key enzyme in lipid A synthesis. The membrane-bound protease FtsH controls the level of LpxC via proteolysis. The C-terminus of LpxC contains a signal sequence necessary for FtsH-dependent degradation Escherichia coli