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Literature summary for 3.5.1.108 extracted from

  • Hernick, M.; Gattis, S.G.; Penner-Hahn, J.E.; Fierke, C.A.
    Activation of Escherichia coli UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase by Fe2+ yields a more efficient enzyme with altered ligand affinity (2010), Biochemistry, 49, 2246-2255.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.5.1.108

Protein Variants

Protein Variants Comment Organism
C63A mutant in which one of the ligands for the inhibitory metal binding site has been removed. The level of inhibition of C63A LpxC by metal ions is significantly reduced, consistent with the Cys63 side chain serving as a ligand for the inhibitory metal ion binding site Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00032
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine wild-type Fe2+-LpxC, pH 7.5, 30°C Escherichia coli
0.0005
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine mutant C63A Fe2+-LpxC, pH 7.5, 30°C Escherichia coli
0.0007
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine mutant C63A Zn2+-LpxC, pH 7.5, 30°C Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ LpxC exhibits 6-8fold higher activity with a single bound Fe2+ as the cofactor compared to Zn2+-LpxC. The catalytic metal ion bound to Fe2+-EcLpxC is five-coordinate. Both metalloenzymes have a bell-shaped dependence on pH with similar pKa values. Ligand affinity of Fe2+-LpxC compared to the Zn2+ enzyme is altered by up to 6fold. In contrast to Zn2+-LpxC, the activity of Fe2+-LpxC is redox-sensitive, and a time-dependent decrease in activity is observed under aerobic conditions Escherichia coli
Zn2+ LpxC exhibits 6-8fold higher activity with a single bound Fe2+ as the cofactor compared to Zn2+-LpxC. Both metalloenzymes have a bell-shaped dependence on pH with similar pKa values. Ligand affinity of Fe2+-LpxC compared to the Zn2+ enzyme is altered by up to 6fold. In contrast to Zn2+-LpxC, the activity of Fe2+-LpxC is redox-sensitive, and a time-dependent decrease in activity is observed under aerobic conditions Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine + H2O
-
 Escherichia coli UDP-3-((R)-3-hydroxytetradecanoyl)-alpha-D-glucosamine + acetate
-
 ?

Synonyms

Synonyms Comment Organism
LpxC
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.5
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine wild-type Fe2+-LpxC, pH 7.5, 30°C Escherichia coli
2.1
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine mutant C63A Zn2+-LpxC, pH 7.5, 30°C Escherichia coli
8.83
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine mutant C63A Fe2+-LpxC, pH 7.5, 30°C Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2833
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine mutant C63A Zn2+-LpxC, pH 7.5, 30°C Escherichia coli
4683
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine wild-type Fe2+-LpxC, pH 7.5, 30°C Escherichia coli
16500
-
 UDP-3-((R)-3-hydroxytetradecanoyl)-N-acetyl-alpha-D-glucosamine mutant C63A Fe2+-LpxC, pH 7.5, 30°C Escherichia coli