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Literature summary extracted from

  • Wang, W.; Maniar, M.; Jain, R.; Jacobs, J.; Trias, J.; Yuan, Z.
    A fluorescence-based homogeneous assay for measuring activity of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (2001), Anal. Biochem., 290, 338-346.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.5.1.108 bovine serum albumin addition of bovine serum albumin slightly increases activity Escherichia coli

Application

EC Number Application Comment Organism
3.5.1.108 medicine LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.108
-
 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.1.108 (4R)-2-(3,4-dimethoxy-5-propylphenyl)-N-hydroxy-4,5-dihydro-1,3-oxazole-4-carboxamide i.e L-161,240 Escherichia coli
3.5.1.108 (4R)-N-hydroxy-2-(4-methoxyphenyl)-4,5-dihydro-1,3-oxazole-4-carboxamide i.e. L-159,692 Escherichia coli
3.5.1.108 EDTA 5 mM, complete loss of activity Escherichia coli
3.5.1.108 Zn2+ 0.1 mM, about 65% loss of activity Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.1.108 0.367
-
 UDP-(2-acetamino)-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose pH 6.0, 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.1.108 Co2+ 0.1 mM, significantly enhances activity Escherichia coli

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 LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UD-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.108 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.108
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.108 UDP-(2-acetamino)-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose + H2O a homogenous fluorescence-based assay is developed that uses UDP–3-O-(N-hexyl-propionamide)-N-acetylglucosamine as a surrogate substrate. This surrogate can be prepared from commercially available UDP-GlcNAc by enzymatic conversion to UDP-MurNAc, which is then chemically coupled to n-hexylamine. Following the LpxC reaction, the free amine of the deacetylation product can be derivatized by fluorescamine, thus generating a fluorescent signal Escherichia coli UDP-2-amino-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose + acetate
-
 ?
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 LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UD-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery Escherichia coli UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?
3.5.1.108 UDP-3-O-(N-hexyl-propionamide)-N-acetylglucosamine + H2O
-
 Escherichia coli ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.1.108 LpxC enzyme
-
 Escherichia coli
3.5.1.108 UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.1.108 0.36
-
 UDP-3-O-(N-hexyl-propionamide)-N-acetylglucosamine pH 6.0, 30°C Escherichia coli

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
3.5.1.108 26
-
 pH 6.0, 30°C, substrate: UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine Escherichia coli (4R)-2-(3,4-dimethoxy-5-propylphenyl)-N-hydroxy-4,5-dihydro-1,3-oxazole-4-carboxamide
3.5.1.108 75
-
 pH 6.0, 30°C, substrate: UDP–3-O-(N-hexyl-propionamide)-N-acetylglucosamine Escherichia coli (4R)-2-(3,4-dimethoxy-5-propylphenyl)-N-hydroxy-4,5-dihydro-1,3-oxazole-4-carboxamide
3.5.1.108 2500
-
 pH 6.0, 30°C, substrate: UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine Escherichia coli (4R)-N-hydroxy-2-(4-methoxyphenyl)-4,5-dihydro-1,3-oxazole-4-carboxamide
3.5.1.108 2600
-
 pH 6.0, 30°C, substrate: UDP–3-O-(N-hexyl-propionamide)-N-acetylglucosamine Escherichia coli (4R)-N-hydroxy-2-(4-methoxyphenyl)-4,5-dihydro-1,3-oxazole-4-carboxamide

General Information

EC Number General Information Comment Organism
3.5.1.108 physiological function LpxC is one of the key enzymes of bacterial lipid A biosynthesis, catalyzing the removal of the N-acetyl group of UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine. The lpxC gene is essential in Gram-negative bacteria but absent from mammalian genomes, making it an attractive target for antibacterial drug discovery Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
3.5.1.108 0.98
-
 UDP-(2-acetamino)-2-deoxy-3-O-[2-(hexylamino)-1-methyl-2-oxoethyl]-D-glucopyranose pH 6.0, 30°C Escherichia coli