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Information on EC 3.5.1.108 - UDP-3-O-acyl-N-acetylglucosamine deacetylase and Organism(s) Aquifex aeolicus and UniProt Accession O67648

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IUBMB Comments
A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.
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Aquifex aeolicus
UNIPROT: O67648
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The taxonomic range for the selected organisms is: Aquifex aeolicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
deacetylase, udp-3-o-(r-3-hydroxymyristoyl)-n-acetylglucosamine deacetylase, deacetylase lpxc, lpxc enzyme, udp-3-o-acyl-n-acetylglucosamine deacetylase, enva protein, udp-3-o-[(r)-3-hydroxymyristoyl]-n-acetylglucosamine deacetylase, udp-3-o-(r-3-hydroxyacyl)-n-acetylglucosamine deacetylase, udp-3-o-[r-3-hydroxymyristoyl]-glcnac deacetylase, lpxc protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deacetylase LpxC
-
LpxC deacetylase
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UDP-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase
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UDP-3-O-(acyl)-N-acetylglucosamine deacetylase
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UDP-3-O-(R-3-hydroxyacyl)-N-acetylglucosamine deacetylase
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UDP-3-O-acyl-N-acetylglucosamine deacetylase
-
UDP-3-O-[(R)-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase
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uridine diphosphate-(3-O-(R-3-hydroxymyristoyl))-N-acetylglucosamine deacetylase
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zinc deacetylase LpxC
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deacetylase 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-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase
-
-
-
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UDP-3-O-acyl-GlcNAc deacetylase
-
-
-
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UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetylglucosamine amidohydrolase
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine amidohydrolase
A zinc protein. The enzyme catalyses a committed step in the biosynthesis of lipid A.
CAS REGISTRY NUMBER
COMMENTARY hide
157971-99-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
show the reaction diagram
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(1-hexanoylamino)-1-oxopropan-2-yl]-alpha-D-glucosamine + acetate
show the reaction diagram
-
-
-
?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
show the reaction diagram
UDP-N-acetylglucosamine + H2O
UDP-D-glucosamine + acetate
show the reaction diagram
-
-
-
?
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
show the reaction diagram
LpxC catalyzes the first committed step in the biosynthesis of lipid A, the hydrophobic anchor of lipopolysaccharide (LPS) that constitutes the outermost monolayer of Gram-negative bacteria. As LpxC is crucial for the survival of Gram-negative organisms and has no sequence homology to known mammalian deacetylases or amidases
-
-
?
UDP-3-O-[(3R)-3-hydroxymyristoyl]-N-acetyl-alpha-D-glucosamine + H2O
UDP-3-O-[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine + acetate
show the reaction diagram
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine + H2O
UDP-3-O-((R)-3-hydroxymyristoyl)-D-glucosamine + acetate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,5-anhydro-2-C-(carboxymethyl-N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol
synthesis of the 13C-labeled substrate-analogue inhibitor, and the subsequent refinement of the solution structure of the LpxC-inhibitor complex using residual dipolar couplings. Structural basis for the design of more potent LpxC inhibitors. The best LpxC inhibitors should contain: (1) a zinc-chelating group situated between two hydrophobic molecular moieties and (2) a negatively charged group or polar group capable of forming salt bridges or hydrogen bonds with the basic patch. For the hydrophobic fragment to fit within the hydrophobic passage, a linear chemical group without branches is preferable and the total length from the hydroxamate group (which presumably binds Zn2+) to the terminal end of the linear fragment should be less than 15 A. Any hydrophobic group with a length beyond 15 A might require flexibility to fit the curved surface extending the hydrophobic passage, where the terminal methyl and the last two methylene groups of the 1,5-anhydro-2-C-(carboxymethyl-N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol acyl chain are located
1,5-anhydro-2-deoxy-2-[2-(hydroxyamino)-2-oxoethyl]-3-O-tetradecanoyl-D-glucitol
the X-ray crystal structure of LpxC complexed with TU-514 allows for a detailed examination of the coordination geometry of the catalytic zinc ion and other enzyme-inhibitor interactions in the active site. The hydroxamate group of TU-514 forms a bidentate chelate complex with the zinc ion and makes hydrogen bond interactions with conserved active site residues E78, H265, and T191. The inhibitor C-4 hydroxyl group makes direct hydrogen bond interactions with E197 and H58. Finally, the C-3 myristate moiety of the inhibitor binds in the hydrophobic tunnel of the active site
4-({4-[(2R,6S)-2,6-dimethylmorpholin-4-yl]phenoxy}methyl)-N-hydroxyoxane-4-carboxamide
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4-({4-[(4-{[(2R,6S)-2,6-dimethylmorpholin-4-yl]methyl}phenyl)ethynyl]phenoxy}methyl)-N-hydroxyoxane-4-carboxamide
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4-({[4-(4-chlorophenoxy)phenyl]sulfanyl}methyl)-N-hydroxyoxane-4-carboxamide
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4-[(4-{2-[(dimethylamino)methyl]morpholin-4-yl}phenoxy)methyl]-N-hydroxyoxane-4-carboxamide
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4-[(4-{[4-({2-[(dimethylamino)methyl]morpholin-4-yl}methyl)phenyl]ethynyl}phenoxy)methyl]-N-hydroxyoxane-4-carboxamide
-
4-{[4-(4-acetylpiperazin-1-yl)phenoxy]methyl}-N-hydroxyoxane-4-carboxamide
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4-{[4-({4-[(4-acetylpiperazin-1-yl)methyl]phenyl}ethynyl)phenoxy]methyl}-N-hydroxyoxane-4-carboxamide
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N,4-dihydroxy-1-{[4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)phenoxy]methyl}cyclohexane-1-carboxamide
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N-((2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl)-4-((4-(morpholinomethyl)phenyl)ethynyl)benzamide
as effectively as ciprofloxacin or tobramycin
N-hydroxy-4-({4-[(4-{[4-(propan-2-yl)piperazin-1-yl]methyl}phenyl)ethynyl]phenoxy}methyl)oxane-4-carboxamide
-
N-hydroxy-4-({4-[4-(propan-2-yl)piperazin-1-yl]phenoxy}methyl)oxane-4-carboxamide
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N-hydroxy-4-({[4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)phenyl]sulfanyl}methyl)oxane-4-carboxamide
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N-hydroxy-4-methoxy-1-{[4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)phenoxy]methyl}cyclohexane-1-carboxamide
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N-hydroxy-4-[(4-{4-[2-(morpholin-4-yl)ethyl]piperazin-1-yl}phenoxy)methyl]oxane-4-carboxamide
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N-hydroxy-4-[(4-{[4-({4-[2-(1H-imidazol-1-yl)ethyl]piperazin-1-yl}methyl)phenyl]ethynyl}phenoxy)methyl]oxane-4-carboxamide
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N-hydroxy-4-[(4-{[4-({4-[2-(morpholin-4-yl)-2-oxoethyl]piperazin-1-yl}methyl)phenyl]ethynyl}phenoxy)methyl]oxane-4-carboxamide
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N-hydroxy-4-[(4-{[4-({4-[2-(morpholin-4-yl)ethyl]piperazin-1-yl}methyl)phenyl]ethynyl}phenoxy)methyl]oxane-4-carboxamide
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N-hydroxy-4-[(4-{[4-({[(4-methoxyphenyl)methyl]amino}methyl)phenyl]ethynyl}phenoxy)methyl]oxane-4-carboxamide
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N-hydroxy-4-{[4-({4-[(4-methylpiperazin-1-yl)methyl]phenyl}ethynyl)phenoxy]methyl}oxane-4-carboxamide
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N-hydroxy-4-{[4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)benzene-1-sulfinyl]methyl}oxane-4-carboxamide
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N-hydroxy-4-{[4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)phenoxy]methyl}oxane-4-carboxamide
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N-[(2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl]-4-({4-[(morpholin-4-yl)methyl]phenyl}ethynyl)benzamide
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(3R,5R)-3-hydroxy-5-(2-(hydroxyamino)-2-oxoethyl)-2-(hydroxymethyl)tetrahydro-2H-pyran-4-yl tetradecanoate
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substrate-analog LpxC inhibitor, possesses little or no antibacterial activity, because it probably cannot penetrate the Gram-negative cell envelope
(R)-3-(5,8-dihydronaphthalen-2-yl)-N-hydroxy-2-(naphthalene-2-sulfonamido)propanamide
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(S)-N-(1-(2-(3,4-dimethoxy-5-propylphenyl)-4,5-dihydrooxazol-4-yl)vinyl)hydroxylamine
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1,5-anhydro-2-C-(carboxymethyl-N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol
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the solution structure of LpxC in complex with the substrate-analog inhibitor 1,5-anhydro-2-C-(carboxymethyl-N-hydroxyamide)-2-deoxy-3-O-myristoyl-D-glucitol, reveals a novel alpha/beta fold, a unique zinc-binding motif and a hydrophobic passage that captures the acyl chain of the inhibitor
Ciprofloxacin
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N-((2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl)-4-((4-(morpholinomethyl)phenyl)ethynyl)benzamide
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N-aroyl-L-threonine hydroxamic acid, antibiotic activity comparable to ciprofloxacin, slow, tight-binding LpxC inhibitor
tobramycin
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additional information
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00065
(3R,5R)-3-hydroxy-5-(2-(hydroxyamino)-2-oxoethyl)-2-(hydroxymethyl)tetrahydro-2H-pyran-4-yl tetradecanoate
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pH 5.5
0.000002
N-((2S,3R)-3-hydroxy-1-(hydroxyamino)-1-oxobutan-2-yl)-4-((4-(morpholinomethyl)phenyl)ethynyl)benzamide
-
-
additional information
(S)-N-(1-(2-(3,4-dimethoxy-5-propylphenyl)-4,5-dihydrooxazol-4-yl)vinyl)hydroxylamine
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Ki value is higher than 500 microM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
assay at
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
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assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the enzyme catalyzes the first committed step of lipid A biosynthesis
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.7 A resolution X-ray crystal structure of LpxC complexed with the substrate analogue inhibitor, 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol, and the 2.0 A resolution structure of LpxC complexed with imidazole. The X-ray crystal structure of LpxC complexed with 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol allows for a detailed examination of the coordination geometry of the catalytic zinc ion and other enzyme-inhibitor interactions in the active site. The hydroxamate group of 1,5-anhydro-2-C-(carboxymethyl-N-hydroxamide)-2-deoxy-3-O-myristoyl-D-glucitol forms a bidentate chelate complex with the zinc ion and makes hydrogen bond interactions with conserved active site residues E78, H265, and T191. The inhibitor C-4 hydroxyl group makes direct hydrogen bond interactions with E197 and H58. Finally, the C-3 myristate moiety of the inhibitor binds in the hydrophobic tunnel of the active site
Aquifex aeolicus LpxC with bound UDP-3-O-(acyl)-glucosamine and with 2 and 9, X-ray diffraction structure determination and analysis. Cocrystal structure of Aquifex aeolicus LpxC with bound product UDP-3-O-(acyl)-glucosamine and Pseudomonas aeruginosa with bound 27b docking model, overview
crystal structure of the LpxC-3-(heptyloxy)benzoate complex
crystallization at 21°C, a sitting drop containing 0.005 ml of protein solution (2.2 mg/ml LpxC, 25 mM Hepes (pH 7.0), 50 mM NaCl, 10 mM magnesium acetate, and 0.5 mM ZnSO4) is equilibrated against a 0.5 ml reservoir of 0.8 M NaCl/0.1 M Hepes (pH 7.0). Crystals of dimensions 0.3 * 0.1 * 0.05 mm3 appear in 5-7 days, larger crystals of dimensions 0.6 * 0.2 * 0.2 mm3 are obtained by macroseeding
crystals of LpxC are grown by hanging-drop vapour diffusion at 20°C, structure of recombinant UDP-3-O-acyl-N-acetylglucosamine deacetylase in complex with UDP, determined to a resolution of 2.2 A. The uracil-binding site is constructed from amino acids that are highly conserved across species. Hydrophobic associations with the Phe155 and Arg250 side chains in combination with hydrogen-bonding interactions with the main chain of Glu154 and the side chains of Tyr151 and Lys227 position the base. The phosphate and ribose groups are directed away from the active site and interact with Arg137, Lys156, Glu186 and Arg250
sitting drop vapor diffusion method, co-crystal structure of the enzyme is solved to 1.6 A resolution
equilibrating a hanging drop containing 0.003 ml of protein solution (3 mg/ml LpxC, 100 mM HEPES, pH 7.5, 180 mM NaCl, 9-14% PEG3350, and 0.5 mM ZnSO4) and 0.003 ml of precipitant buffer (100 mM HEPES, pH 7.5, 180 mM NaCl, 9-14% PEG3350, and 0.5 mM ZnSO4) over a reservoir containing about 1 ml of precipitant buffer. Crystals with maximum dimensions of 0.3 * 0.15 * 0.15 mm3 grow within 3 days and are gradually transferred to a stabilization buffer of 100 mM sodium cacodylate, pH 6.0, 180 mM NaCl, 11-16% PEG 3350, 0.5 mM ZnSO4, and 1% glycerol. Crystals are flash-cooled in liquid nitrogen following cryoprotection with 22% glycerol and diffracted X-rays to 2.1 Å. Crystals are isomorphous with those prepared at pH 7.0 and belong to space group P6(1) with unit cell dimensions a = b = 101.3 A, c = 122.7 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C193A/DELTAD284-L294
variant of LpxC
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
D105A
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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
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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
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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
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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
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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
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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
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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
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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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
-
stable for up to 20 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
C193A/DELTAD284-L294 variant of LpxC
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C193A/DELTAD284-L294 variant of LpxC overexpressed in Escherichia coli
expression in Escherichia coli BL21(DE3)
overepression of LpxC variants in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
drug development
-
lipid A is an essential component of the outer membranes of most Gram-negative bacteria, making LpxC an attractive target for antibiotic design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buetow, L.; Dawson, A.; Hunter, W.N.
The nucleotide-binding site of Aquifex aeolicus LpxC
Acta Crystallogr. Sect. F
62
1082-1086
2006
Aquifex aeolicus (O67648), Aquifex aeolicus
Manually annotated by BRENDA team
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
Biochemistry
40
514-523
2001
Aquifex aeolicus, Escherichia coli
Manually annotated by BRENDA team
Coggins, B.E.; McClerren, A.L.; Jiang, L.; Li, X.; Rudolph, J.; Hindsgaul, O.; Raetz, C.R.; Zhou, P.
Refined solution structure of the LpxC-TU-514 complex and pKa analysis of an active site histidine: insights into the mechanism and inhibitor design
Biochemistry
44
1114-1126
2005
Aquifex aeolicus (O67648), Aquifex aeolicus
Manually annotated by BRENDA team
McClerren, A.L.; Endsley, S.; Bowman, J.L.; Andersen, N.H.; Guan, Z.; Rudolph, J.; Raetz, C.R.
A slow, tight-binding inhibitor of the zinc-dependent deacetylase LpxC of lipid A biosynthesis with antibiotic activity comparable to ciprofloxacin
Biochemistry
44
16574-16583
2005
Aquifex aeolicus, Escherichia coli, Escherichia coli R477
Manually annotated by BRENDA team
Gennadios, H.A.; Whittington, D.A.; Li, X.; Fierke, C.A.; Christianson, D.W.
Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase
Biochemistry
45
7940-7948
2006
Aquifex aeolicus (O67648)
Manually annotated by BRENDA team
Shin, H.; Gennadios, H.A.; Whittington, D.A.; Christianson, D.W.
Amphipathic benzoic acid derivatives: synthesis and binding in the hydrophobic tunnel of the zinc deacetylase LpxC
Bioorg. Med. Chem.
15
2617-2623
2007
Aquifex aeolicus (O67648)
Manually annotated by BRENDA team
Hernick, M.; Gennadios, H.A.; Whittington, D.A.; Rusche, K.M.; Christianson, D.W.; Fierke, C.A.
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism
J. Biol. Chem.
280
16969-16978
2005
Escherichia coli, Aquifex aeolicus (O67848), Aquifex aeolicus
Manually annotated by BRENDA team
Robinet, J.J.; Gauld, J.W.
DFT investigation on the mechanism of the deacetylation reaction catalyzed by LpxC
J. Phys. Chem. B
112
3462-3469
2008
Aquifex aeolicus
Manually annotated by BRENDA team
Coggins, B.E.; Li, X.; McClerren, A.L.; Hindsgaul, O.; Raetz, C.R.; Zhou, P.
Structure of the LpxC deacetylase with a bound substrate-analog inhibitor
Nat. Struct. Biol.
10
645-651
2003
Aquifex aeolicus
Manually annotated by BRENDA team
Whittington, D.A.; Rusche, K.M.; Shin, H.; Fierke, C.A.; Christianson, D.W.
Crystal structure of LpxC, a zinc-dependent deacetylase essential for endotoxin biosynthesis
Proc. Natl. Acad. Sci. USA
100
8146-8150
2003
Aquifex aeolicus (O67648), Aquifex aeolicus
Manually annotated by BRENDA team
Barb, A.W.; Jiang, L.; Raetz, C.R.; Zhou, P.
Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding
Proc. Natl. Acad. Sci. USA
104
18433-18438
2007
Escherichia coli, Aquifex aeolicus (O67648), Rhizobium leguminosarum (Q1ME43)
Manually annotated by BRENDA team
Murphy-Benenato, K.; Olivier, N.; Choy, A.; Ross, P.; Miller, M.; Thresher, J.; Gao, N.; Hale, M.
Synthesis, structure, and SAR of tetrahydropyran-based LpxC inhibitors
ACS Med. Chem. Lett.
5
1213-1218A
2014
Escherichia coli, Pseudomonas aeruginosa, Aquifex aeolicus (O67648), Aquifex aeolicus, Escherichia coli W3110 / ATCC 27325
Manually annotated by BRENDA team
Kalinin, D.V.; Holl, R.
Insights into the zinc-dependent deacetylase LpxC biochemical properties and inhibitor design
Curr. Top. Med. Chem.
16
2379-2430
2016
Aquifex aeolicus (O67648), Escherichia coli (P0A727), Pseudomonas aeruginosa (P47205), Pseudomonas aeruginosa ATCC 15692 (P47205)
Manually annotated by BRENDA team
Miller, M.; Gao, N.; Ross, P.; Olivier, N.
Crystal structure of A. aeolicus LpxC with bound product suggests alternate deacetylation mechanism
Proteins
83
1706-1719
2015
Aquifex aeolicus (O67648), Aquifex aeolicus
Manually annotated by BRENDA team