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Literature summary for 3.5.1.108 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

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

Application

Application Comment Organism
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)

Cloned (Comment) Organism
-
Escherichia coli

Inhibitors

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Metals/Ions Comment Organism Structure
Co2+ 0.1 mM, significantly enhances activity 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 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

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
?
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 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
-
?
UDP-3-O-(N-hexyl-propionamide)-N-acetylglucosamine + H2O
-
Escherichia coli ?
-
?

Synonyms

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

Turnover Number [1/s]

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

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
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
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
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
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

General Information Comment Organism
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]

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