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3.5.1.108: UDP-3-O-acyl-N-acetylglucosamine deacetylase

This is an abbreviated version!
For detailed information about UDP-3-O-acyl-N-acetylglucosamine deacetylase, go to the full flat file.

Word Map on EC 3.5.1.108

Reaction

a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine
+
H2O
=
a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
 +
acetate

Synonyms

deacetylase, deacetylase LpxC, DHTase, EnvA protein, LpxC, LpxC deacetylase, LpxC enzyme, LpxC protein, UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase, UDP-(3-O-acyl)-N-acetylglucosamine deacetylase, UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, UDP-3-O-(acyl)-N-acetylglucosamine deacetylase, UDP-3-O-(R-3-hydroxyacyl)-N-acetylglucosamine deacetylase, UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc deacetylase, UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, UDP-3-O-(R-3-hydroxymyristoyl)-Nacetylglucosamine deacetylase, UDP-3-O-acyl-GlcNAc deacetylase, UDP-3-O-acyl-N-acetylglucosamine deacetylase, UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase, UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase, UDP-3-O-[R-3-hydroxymyristoyl]-GlcNAc deacetylase, UDP-3-O-[R-3-hydroxymyristoyl]-GlcNAc deacetylase enzyme, uridine diphosphate-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase, zinc deacetylase LpxC

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.108 UDP-3-O-acyl-N-acetylglucosamine deacetylase

Engineering

Engineering on EC 3.5.1.108 - UDP-3-O-acyl-N-acetylglucosamine deacetylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C193A/DELTAD284-L294
variant of LpxC
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
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
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
D246A
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
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
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
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
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
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
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
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
E78A/H265A
decrease in kcat/KM compared to wild-type Zn2+-containing enzyme
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
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
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
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
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
H265A
decrease in kcat/KM compared to wild-type Zn2+-containing enzyme
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
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
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
K227E
-
completely inactive mutant enzyme
T179A
LpxC mutant is less sensitive to N-((2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl)-4-((4-(morpholinomethyl)phenyl)ethynyl)benzamide inhibition
C125A
-
as sensitive to 2,3,4-trihydroxybenzaldehyde O-((2R,3R,4S,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl oxime as the wild-type enzyme
C125S
-
site-directed mutagenesis, crystal structure analysis
C207A
-
much less sensitive to 2,3,4-trihydroxybenzaldehyde O-((2R,3R,4S,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl oxime inhibition, suggesting that Cys-207 is necessary to form the E-I complex
C214N
-
as sensitive to 2,3,4-trihydroxybenzaldehyde O-((2R,3R,4S,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl oxime as the wild-type enzyme
C250A
-
as sensitive to 2,3,4-trihydroxybenzaldehyde O-((2R,3R,4S,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl oxime as the wild-type enzyme
C63S
-
as sensitive to 2,3,4-trihydroxybenzaldehyde O-((2R,3R,4S,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl oxime as the wild-type enzyme
C65A
-
as sensitive to 2,3,4-trihydroxybenzaldehyde O-((2R,3R,4S,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl oxime as the wild-type enzyme
D197A
-
site-directed mutagenesis
D197E
-
site-directed mutagenesis
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
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
D246A
E78A/H265A
-
14800fold decrease in kcat/KM compared to wild-type Zn2+-containing enzyme
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
F192A
-
site-directed mutagenesis
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
H265A
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
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
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
I38T
-
lpxC gene
K143A
-
site-directed mutagenesis
K239A
-
site-directed mutagenesis
N162A
-
site-directed mutagenesis
Q202W/G210S
T191A
-
site-directed mutagenesis
I38T
-
lpxC gene
-
G17S
-
partially-inactivated LpxC mutant G17S
-
C40S
site-directed mutagenesis, crystal structure analysis
S214G
completely inhibited by 0.5 microM N-((2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl)-4-((4-(morpholinomethyl)phenyl)ethynyl)benzamide, wild-type under the same conditions 50% inhibited
W206Q/S214G
completely inhibited by 0.5 microM N-((2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl)-4-((4-(morpholinomethyl)phenyl)ethynyl)benzamide, wild-type under the same conditions 50% inhibited
additional information