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Literature summary for 3.5.1.108 extracted from

  • Jackman, J.E.; Raetz, C.R.; Fierke, C.A.
    Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding site (2001), Biochemistry, 40, 514-523.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overepression of LpxC variants in Escherichia coli Escherichia coli
overepression of LpxC variants in Escherichia coli Aquifex aeolicus

Protein Variants

Protein Variants Comment Organism
D105A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 56% of the specific activity of the wild-type extract Aquifex aeolicus
D105N expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 67% of the specific activity of the wild-type extract Aquifex aeolicus
D105S expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 78% of the specific activity of the wild-type extract Aquifex aeolicus
D242A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 9.5% of the specific activity of the wild-type extract Escherichia coli
D242Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.04% of the specific activity of the wild-type extract Escherichia coli
D246A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.001% of the specific activity of the wild-type extract. Contains 64% Fe2+ compared to wild-type Zn2+ content Aquifex aeolicus
D246A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.06% of the specific activity of the wild-type extract Escherichia coli
D246N expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 3.5% of the specific activity of the wild-type extract Aquifex aeolicus
D246S expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about less than 0.0005% of the specific activity of the wild-type extract Aquifex aeolicus
E100A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 72% of the specific activity of the wild-type extract Aquifex aeolicus
E100N expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 61% of the specific activity of the wild-type extract Aquifex aeolicus
E100S expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 83% of the specific activity of the wild-type extract Aquifex aeolicus
E234A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 4.8% of the specific activity of the wild-type extract Aquifex aeolicus
E234N expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about less than 0.0005% of the specific activity of the wild-type extract Aquifex aeolicus
E234S expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 6.7% of the specific activity of the wild-type extract Aquifex aeolicus
E78A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.1% of the specific activity of the wild-type extract Escherichia coli
E78A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 9.8% of the specific activity of the wild-type extract. Contains 28% Fe2+ compared to wild-type Zn2+ content. The specific activity of the E78A LpxC variant is neither inhibited nor activated by the addition of up to 1 mM Zn2+ Aquifex aeolicus
E78Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.03% of the specific activity of the wild-type extract Escherichia coli
E78Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about less than 0.0005% of the specific activity of the wild-type extract Aquifex aeolicus
H19A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.07% of the specific activity of the wild-type extract. Escherichia coli
H19A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 5% of the specific activity of the wild-type extract. Contains 51% Fe2+ compared to wild-type Zn2+ content Aquifex aeolicus
H19Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 1.1% of the specific activity of the wild-type extract Escherichia coli
H19Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 45% of the specific activity of the wild-type extract Aquifex aeolicus
H19Y expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.5% of the specific activity of the wild-type extract Escherichia coli
H19Y expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 4.4% of the specific activity of the wild-type extract Aquifex aeolicus
H238A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.09% of the specific activity of the wild-type extract Escherichia coli
H238A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.1% of the specific activity of the wild-type extract. Extract overexpressing H238A is stimulated approximately 20fold by the addition of ZnSO4 Aquifex aeolicus
H265A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.03% of the specific activity of the wild-type extract Escherichia coli
H265Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.02% of the specific activity of the wild-type extract Escherichia coli
H265Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about less than 0.0005% of the specific activity of the wild-type extract Aquifex aeolicus
H79A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.006% of the specific activity of the wild-type extract. Contains 10% Fe2+ compared to wild-type Zn2+ content. Extract overexpressing H79A is stimulated approximately 20fold by the addition of ZnSO4 Aquifex aeolicus
H79A expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.04% of the specific activity of the wild-type extract Escherichia coli
H79Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.008% of the specific activity of the wild-type extract Aquifex aeolicus
H79Q expressed to level comparable to wild-type LpxC. The extract overexpressing LpxC exhibits about 0.08% of the specific activity of the wild-type extract Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Zn2+
-
Aquifex aeolicus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ the low activity of LpxC variants at positions H79 and H238, coupled with the ability of Zn2+ to stimulate the activity of these enzymes and the low Zn2+ content of the purified variant enzymes suggests that these residues directly coordinate a catalytic Zn2+ in LpxC. The variants with alanine substituted at H265 or D246 also exhibit large decreases in LpxC activity, suggesting that one of these residues may constitute a third protein ligand to the active-site Zn2+ Escherichia coli
Zn2+ wild-type enzyme contains 0.98 mg of Zn2+ per g of protein. The low activity of LpxC variants at positions H79 and H238, coupled with the ability of Zn2+ to stimulate the activity of these enzymes and the low Zn2+ content of the purified variant enzymes suggests that these residues directly coordinate a catalytic Zn2+ in LpxC. The variants with alanine substituted at H265 or D246 also exhibit large decreases in LpxC activity, suggesting that one of these residues may constitute a third protein ligand to the active-site Zn2+ 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 Escherichia coli LpxC catalyzes a step in the biosynthesis of lipid A in Gram-negative bacteria UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O Aquifex aeolicus LpxC catalyzes a step in the biosynthesis of lipid A in Gram-negative bacteria UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
?

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus
-
-
-
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Aquifex aeolicus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.84
-
-
Escherichia coli
0.84
-
-
Aquifex aeolicus

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
-
Aquifex aeolicus UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O LpxC catalyzes a step in the biosynthesis of lipid A in Gram-negative bacteria Escherichia coli UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O LpxC catalyzes a step in the biosynthesis of lipid A in Gram-negative bacteria Aquifex aeolicus UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
?

Synonyms

Synonyms Comment Organism
LpxC protein
-
Escherichia coli
LpxC protein
-
Aquifex aeolicus
UDP-(3-O-acyl)-N-acetylglucosamine deacetylase
-
Escherichia coli
UDP-(3-O-acyl)-N-acetylglucosamine deacetylase
-
Aquifex aeolicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Escherichia coli
60
-
assay at Aquifex aeolicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
6 h, stable Escherichia coli
60
-
stable for up to 20 min Aquifex aeolicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
assay at Aquifex aeolicus
5.9
-
assay at Escherichia coli