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Literature summary for 3.5.1.108 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)

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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
-
?
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
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
-
Escherichia coli UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
?
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
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
-
Escherichia coli W3110 / ATCC 27325 UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
?
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

Synonyms Comment Organism
LpxC protein
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Escherichia coli

General Information

General Information Comment Organism
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