Literature summary for 3.5.1.108 extracted from

Coggins, B.E.; McClerren, A.L.; Jiang, L.; Li, X.; Rudolph, J.; Hindsgaul, O.; Raetz, C.R.; Zhou, P.
Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design (2005), Biochemistry, 44, 1114-1126.

Search for more literature for 3.5.1.108

Inhibitors

Inhibitors	Comment	Organism	Structure
1,5-anhydro-2-C-(carboxymethyl-N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol	synthesis of the 13C-labeled substrate-analogue inhibitor, and the subsequent refinement of the solution structure of the LpxC-inhibitor complex using residual dipolar couplings. Structural basis for the design of more potent LpxC inhibitors. The best LpxC inhibitors should contain: (1) a zinc-chelating group situated between two hydrophobic molecular moieties and (2) a negatively charged group or polar group capable of forming salt bridges or hydrogen bonds with the basic patch. For the hydrophobic fragment to fit within the hydrophobic passage, a linear chemical group without branches is preferable and the total length from the hydroxamate group (which presumably binds Zn2+) to the terminal end of the linear fragment should be less than 15 A. Any hydrophobic group with a length beyond 15 A might require flexibility to fit the curved surface extending the hydrophobic passage, where the terminal methyl and the last two methylene groups of the 1,5-anhydro-2-C-(carboxymethyl-N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol acyl chain are located	Aquifex aeolicus

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	Aquifex aeolicus	LpxC catalyzes the first committed step in the biosynthesis of lipid A, the hydrophobic anchor of lipopolysaccharide (LPS) that constitutes the outermost monolayer of Gram-negative bacteria. As LpxC is crucial for the survival of Gram-negative organisms and has no sequence homology to known mammalian deacetylases or amidases	UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate	-	?

Organism

Organism	UniProt	Comment	Textmining
Aquifex aeolicus	O67648	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O	-	Aquifex aeolicus	UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate	-	?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O	LpxC catalyzes the first committed step in the biosynthesis of lipid A, the hydrophobic anchor of lipopolysaccharide (LPS) that constitutes the outermost monolayer of Gram-negative bacteria. As LpxC is crucial for the survival of Gram-negative organisms and has no sequence homology to known mammalian deacetylases or amidases	Aquifex aeolicus	UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate	-	?

Synonyms

Synonyms	Comment	Organism
LpxC deacetylase	-	Aquifex aeolicus
UDP-3-O-acyl-N-acetylglucosamine deacetylase	-	Aquifex aeolicus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)