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Literature summary for 3.5.1.108 extracted from

  • Jackman, J.E.; Raetz, C.R.; Fierke, C.A.
    UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase of Escherichia coli is a zinc metalloenzyme (1999), Biochemistry, 38, 1902-1911.
    View publication on PubMed
Search for more literature for 3.5.1.108

Inhibitors

Inhibitors Comment Organism Structure
dipicolinic acid 0.02 mM, complete inhibition Escherichia coli
EDTA t1/2: 4 min at 0.005 mM EDTA at 1 °C Escherichia coli
additional information incubation of 10 nM LpxC in buffer without bovine serum albumin for 30 min completely inactivates the enzyme. When this enzyme is diluted further (4fold) into buffer containing 1 mg/ml bovine serum albumin, 100% of the activity is restored when assayed after a 2 h incubation. High concentrations of LpxC in the assays can eliminate the requirement of bovine serum albumin Escherichia coli
Zn2+
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0006
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine pH 5.7, 1°C Escherichia coli
0.0021
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine pH 5.5, 30°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+) Escherichia coli
Mn2+ incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+) Escherichia coli
Ni2+ incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+) Escherichia coli
Zn2+ incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+) Escherichia coli
Zn2+ LpxC is a metalloenzyme that requires bound Zn2+ for optimal activity. The actual concentration of bound Zn2+ varies with different enzyme preparations from 1.3-3.2 mol of Zn2+/mol of LpxC with an average Zn2+ content of about 2 mol of Zn2+/mol of LpxC. No other bound metal ions are detected in purified LpxC. The bound Zn2+ can be removed from LpxC by incubation with DPA, and the bound zinc ions can be easily reconstituted by incubation with Zn2+. Reconstitution of LpxC in presence of Cd2+, Ca2+, Cu2+, or Mg2+ is equal to or below the activity of apo-LpxC, indicating that these metal ions are ineffective at substituting for Zn2+. Incubation of apo-LpxC (0.125 mM) with stoichiometric amounts of Mn2+, Co2+, and Ni2+ reactivates apo-LpxC to varying degrees (Co2+, Ni2+ > Zn2+ > Mn2+) 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
-
 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-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
-
 Escherichia coli UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?
UDP-N-acetyl-alpha-D-glucosamine + H2O kcat/KM fo UDP-N-acetylglucosamine is 5000000-fold lower than the kcat/Km for UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine Escherichia coli UDP-alpha-D-glucosamine + acetate
-
 ?

Synonyms

Synonyms Comment Organism
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
0.09
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine pH 5.7, 1°C Escherichia coli
3.3
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine pH 5.5, 30°C Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.007
-
 40 mM Bis-Tris, pH 6 at 1°C Escherichia coli Zn2+
0.024
-
 40 mM Bis-Tris, pH 5.5 at 30°C Escherichia coli Zn2+

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.00028
-
 UDP-N-acetylglucosamine pH 5.7, 30°C Escherichia coli
140
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine pH 5.7, 1°C Escherichia coli
1500
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine pH 5.5, 30°C Escherichia coli