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Literature summary for 3.5.1.108 extracted from

  • Hernick, M.; Fierke, C.A.
    Catalytic mechanism and molecular recognition of E. coli UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase probed by mutagenesis (2006), Biochemistry, 45, 15240-15248.
    View publication on PubMed
Search for more literature for 3.5.1.108

Application

Application Comment Organism
drug development LpxC is a target for the development of antimicrobial agents in the treatment of Gram negative infections Escherichia coli

Protein Variants

Protein Variants Comment Organism
D197A site-directed mutagenesis Escherichia coli
D197E site-directed mutagenesis Escherichia coli
F192A site-directed mutagenesis Escherichia coli
H19A site-directed mutagenesis Escherichia coli
H19Q site-directed mutagenesis Escherichia coli
H19Y site-directed mutagenesis Escherichia coli
K143A site-directed mutagenesis Escherichia coli
K239A site-directed mutagenesis Escherichia coli
N162A site-directed mutagenesis Escherichia coli
T191A site-directed mutagenesis Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00019
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine wild-type Escherichia coli
0.0005
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine F192A mutant Escherichia coli
0.0008
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine D197E mutant Escherichia coli
0.0008
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine K239A mutant Escherichia coli
0.0011
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine D197A mutant Escherichia coli
0.0013
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19A mutant Escherichia coli
0.0016
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine T191A mutant Escherichia coli
0.0024
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19Q mutant Escherichia coli
0.011
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19Y mutant Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ metal-dependent deacetylase Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli catalyzes the second step in the biosynthesis of lipid A ?
-
 ?

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.
additional information catalyzes the second step in the biosynthesis of lipid A Escherichia coli ?
-
 ?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
-
 Escherichia coli UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
-
 ?

Synonyms

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

Temperature Optimum [°C]

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.01
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine K239A mutant Escherichia coli
0.017
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19A mutant Escherichia coli
0.052
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine F192A mutant Escherichia coli
0.053
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine T191A mutant Escherichia coli
0.13
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19Q mutant Escherichia coli
0.25
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19Y mutant Escherichia coli
1.32
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine D197E mutant Escherichia coli
1.5
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine wild-type Escherichia coli
1.5
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine D197A mutant Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 affinity of EcLpxC for the product (myrUDP-GlcNH2) is determined as a function of pH to ascertain whether there are ionizations important for binding affinity. For wild-type LpxC, the KD product value increases at both low and high pH in a log-linear fashion, indicating that two ionizations affect binding affinity Escherichia coli
7.5
-
 assay at Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.31
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19A mutant, 575fold decrease Escherichia coli
12.5
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine K239A mutant, 575fold decrease Escherichia coli
22.73
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19Y mutant, 350fold decrease Escherichia coli
33.13
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine K143A mutant, 700fold decrease Escherichia coli
54.17
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine H19Q mutant, 135fold decrease Escherichia coli
104
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine F192A mutant, 1200fold decrease Escherichia coli
1364
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine D197A mutant, 5fold decrease Escherichia coli
1650
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine D197E mutant, 5fold decrease Escherichia coli
7895
-
 UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine wild-type Escherichia coli