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Information on EC 3.6.1.54 - UDP-2,3-diacylglucosamine diphosphatase
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EC Tree
3.6.1.54 UDP-2,3-diacylglucosamine diphosphataseIUBMB Comments
The enzyme catalyses a step in the biosynthesis of lipid A.
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Word Map
- 3.6.1.54
- lipopolysaccharide
- pyrophosphate
- influenzae
-
haemophilus
- ump
-
phosphoesterase
-
calcineurin-like
- leaflet
- piperazine
-
sulfonyl
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
=
+
a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine
+
=
+
Synonyms
udp-2,3-diacylglucosamine pyrophosphatase, udp-2,3-diacylglucosamine hydrolase, udp-diacylglucosamine pyrophosphohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LpxH
LpxI
UDP-2,3-bis[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine 2,3-bis[(3R)-3-hydroxymyristoyl]-beta-D-glucosaminyl 1-phosphate phosphohydrolase
-
-
incorrect
-
UDP-2,3-diacylglucosamine hydrolase
UDP-2,3-diacylglucosamine pyrophosphatase
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate phosphohydrolase
-
-
-
-
UDP-diacylglucosamine pyrophosphohydrolase
YbbF
LpxH
-
-
-
-
UDP-2,3-diacylglucosamine hydrolase
-
-
-
-
UDP-2,3-diacylglucosamine pyrophosphatase
-
-
-
-
YbbF
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H2O = a lipid X + UMP
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine 2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine-1-phosphate phosphohydrolase
The enzyme catalyses a step in the biosynthesis of lipid A.
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CAS REGISTRY NUMBER
COMMENTARY
469863-59-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
UDP-N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + H2O
N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine 1-phosphate + UMP
strict requirement for a diacylated substrate. LpxH hydrolysis incorporates H218O into UMP by catalyzing the attack of water on the alpha-phosphorus atom of UDP-2,3-diacylglucosamine
-
-
?
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
-
a step of lipid A biosynthesis. LpxH is essential in Escherichia coli
-
-
?
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
step of lipid A biosynthesis
-
-
?
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
-
step of lipid A biosynthesis. Pseudomonas aeruginosa LpxH catalyzes UDP-2,3-diacylglucosamine hydrolysis in vitro and can substitute for Escherichia coli lpxH in vivo
-
-
?
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
-
Pseudomonas aeruginosa LpxH catalyzes UDP-2,3-diacylglucosamine hydrolysis in vitro and can substitute for Escherichia coli lpxH in vivo
-
-
?
UDP-2,3-diacylglucosamine + H2O
2,3-diacylglucosamine 1-phosphate + UMP
the enzyme is selective for UDP-2,3-diacylglucosamine
-
-
?
UDP-2,3-diacylglucosamine + H2O
2,3-diacylglucosamine 1-phosphate + UMP
the enzyme is selective for UDP-2,3-diacylglucosamine
-
-
?
UDP-2,3-diacylglucosamine + H2O
2,3-diacylglucosamine 1-phosphate + UMP
-
-
-
?
UDP-2,3-diacylglucosamine + H2O
2,3-diacylglucosamine 1-phosphate + UMP
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
?
additional information
?
-
cytoplasmic cyclophilin PPIB physically interacts with UDP-2, 3-diacylglucosamine hydrolase LpxH
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-
?
additional information
?
-
no activity with UDP-N-acetylglucosamine and UDP-3-O-(R)-(3-hydroxymyristoyl)glucosamine, LpxH does not cleave CDP-diacylglycerol
-
-
?
additional information
?
-
-
no activity with UDP-N-acetylglucosamine and UDP-3-O-(R)-(3-hydroxymyristoyl)glucosamine, LpxH does not cleave CDP-diacylglycerol
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
-
a step of lipid A biosynthesis. LpxH is essential in Escherichia coli
-
-
?
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
step of lipid A biosynthesis
-
-
?
UDP-2,3-bis((3R)-3-hydroxymyristoyl)alpha-D-glucosamine + H2O
2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate + UMP
-
step of lipid A biosynthesis. Pseudomonas aeruginosa LpxH catalyzes UDP-2,3-diacylglucosamine hydrolysis in vitro and can substitute for Escherichia coli lpxH in vivo
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
-
?
UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine + H2O
2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + UMP
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
Fe3+
10-50fold stimulation compared to conditions without metal additive
Mg2+
the apparent specific activity of purified enzyme increases 10fold in the presence of Mg2+ versus no added metal. Enzyme activity is maximal at 0.2 mM Mg2+ and remains approximately the same up to 20 mM Mg2+
Mn2+
Ni2+
10-50fold stimulation compared to conditions without metal additive
Co2+
the apparent specific activity of purified enzyme increases 6fold in the presence of added Co2+
Co2+
10-50fold stimulation compared to conditions without metal additive
Mn2+
the apparent specific activity of purified enzyme increases 6fold in the presence of added Mn2+
Mn2+
600fold stimulation in presence of Mn2+, optimum concentraion 2.5 mM. Presence of a di-Mn2+ cluster
Mn2+
contains two Mn2+ ions which are required for enzymatic activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(5-((4-(3-(trifluoromethyl) phenyl)piperazin-1-yl) sulfonyl)indolin-1-yl)ethan-1-one
47.2% residual activity at 0.002 mM, 23.5% residual activity at 0.006 mM, 14.1% residual activity at 0.01 mM, 11.7% residual activity at 0.05 mM
1-(5-[4-[3-(propan-2-yl)phenyl]piperazine-1-carbonyl]-2,3-dihydro-1H-indol-1-yl)ethan-1-one
-
29% residual activity at 0.01 mM
1-(5-[4-[3-(trifluoromethyl)phenyl]-1,4-diazepane-1-sulfonyl]-2,3-dihydro-1H-indol-1-yl)ethan-1-one
-
94% residual activity at 0.01 mM
1-(5-[4-[3-(trifluoromethyl)phenyl]piperazine-1-sulfonyl]-2,3-dihydro-1H-indol-1-yl)ethan-1-one
-
6.0% residual activity at 0.01 mM
1-[5-(4-phenylpiperazine-1-sulfonyl)-2,3-dihydro-1H-indol-1-yl]ethan-1-one
-
32% residual activity at 0.01 mM
1-[5-(4-[[3-(trifluoromethyl)phenyl]methyl]piperazine-1-carbonyl)-2,3-dihydro-1H-indol-1-yl]ethan-1-one
-
87% residual activity at 0.01 mM
1-[5-[4-(3-bromophenyl)piperazine-1-sulfonyl]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
-
24% residual activity at 0.01 mM
1-[5-[4-(3-ethylphenyl)piperazine-1-carbonyl]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
-
21% residual activity at 0.01 mM
1-[5-[4-(3-hydroxyphenyl)piperazine-1-sulfonyl]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
-
91% residual activity at 0.01 mM
1-[5-[4-([1,1'-biphenyl]-3-yl)piperazine-1-carbonyl]-2,3-dihydro-1H-indol-1-yl]ethan-1-one
-
24% residual activity at 0.01 mM
2-oxo-2-((4-((4-(3-(trifluoromethyl)phenyl)piperazin-1-yl)sulfonyl)phenyl)amino)acetic acid
-
55% residual activity at 0.01 mM
3-[4-[3-(trifluoromethyl)phenyl]piperazine-1-sulfonyl]benzoic acid
-
98% residual activity at 0.01 mM
4-[5-[4-(3-bromophenyl)piperazine-1-sulfonyl]-2,3-dihydro-1H-indol-1-yl]-4-oxobutanoic acid
-
24% residual activity at 0.01 mM
methyl 4-[5-[4-(3-bromophenyl)piperazine-1-sulfonyl]-2,3-dihydro-1H-indol-1-yl]-4-oxobutanoate
-
42% residual activity at 0.01 mM
N-(4-((4-(3-(trifluoromethyl)phenyl)piperazin-1-yl)sulfonyl)phenyl)acetamide
-
36% residual activity at 0.01 mM
N-(4-[4-[3-(trifluoromethyl)phenyl]piperazine-1-sulfonyl]phenyl)acetamide
-
30% residual activity at 0.01 mM
N1-hydroxy-N2-(4-((4-(3-(trifluoromethyl)phenyl)piperazin-1-yl)sulfonyl)phenyl)oxalamide
-
41% residual activity at 0.01 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Triton X-100
stimulation in hydrolysis as the detergent concentration approaches the critical micelle concentration of 0.19 mM
additional information
enzyme is active without addition of detergent
-
additional information
-
enzyme is active without addition of detergent
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Whooping Cough
Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0617
UDP-N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
pH 8.0, 30°C
0.105
UDP-2,3-diacylglucosamine
in 100 mM sodium acetate, 50 mM bis(2-hydroxyethyl)imino-tris(hydroxymethyl)hexane, and 50 mM Tris, 2 mM MgCl2, at 30°C, pH not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0012
1-(5-((4-(3-(trifluoromethyl) phenyl)piperazin-1-yl) sulfonyl)indolin-1-yl)ethan-1-one
Escherichia coli
at pH 8.0 and 30°C
0.000147
1-(5-[4-[3-(trifluoromethyl)phenyl]piperazine-1-sulfonyl]-2,3-dihydro-1H-indol-1-yl)ethan-1-one
Escherichia coli
-
at pH 8.0 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
membane-free lysate, in 100 mM sodium acetate, 50 mM bis(2-hydroxyethyl)imino-tris(hydroxymethyl)hexane, and 50 mM Tris, 2 mM MgCl2, at 30°C, pH not specified in the publication
30
after 1.2fold purification, in 100 mM sodium acetate, 50 mM bis(2-hydroxyethyl)imino-tris(hydroxymethyl)hexane, and 50 mM Tris, 2 mM MgCl2, at 30°C, pH not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
assay at. Enzyme is most active at slightly alkaline pH values and exhibits a sharp decrease in its catalytic activity at low pH
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
pH 6.5: about 50% of maximal activity, pH 9.5: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
construction of Escherichia coli mutant KB21/pKJB5 that contains a kanamycin cassette inserted into the chromosomal copy of lpxH. The plasmid pKJB5 harbors lpxH+ and features a temperature-sensitive origin of replication. KB21/pKJB5 grows on nutrient medium at 30 °C but not at 44 °C when the plasmid carrying lpxH+ is lost. It is conclude that lpxH is essential in Escherichia coli
malfunction
UDP-2,3-diacylglucosamine-deficiency results in lethality
malfunction
blockage of LpxH causes accumulation of detergent-like pathway intermediates that prevents cell growth
malfunction
enzyme depletion causes clear morphological defects in Acinetobacter baumannii strain ATCC 19606
malfunction
-
UDP-2,3-diacylglucosamine-deficiency results in lethality
-
malfunction
-
enzyme depletion causes clear morphological defects in Acinetobacter baumannii strain ATCC 19606
-
malfunction
-
blockage of LpxH causes accumulation of detergent-like pathway intermediates that prevents cell growth
-
metabolism
the enzyme is involved in lipid A biosynthesis. The enzyme is essential for growth in the strain Acinetobacter baumannii ATCC 19606
metabolism
-
the enzyme is involved in lipid A biosynthesis. The enzyme is essential for growth in the strain Acinetobacter baumannii ATCC 19606
-
physiological function
the enzyme is essential for growth in Acinetobacter baumannii strain ATCC 19606
physiological function
-
the enzyme is essential for growth in Acinetobacter baumannii strain ATCC 19606
-
Show AA Sequence and Transmembrane Helices (10236 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme F141H/L142S/L146S/F147H/E14A/E15A/K161T/E162A, hanging drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.2, 70-80 mM magnesium formate and 1-5% (v/v) 2-propanol
in complex with lipid X, using 100 mM NaCl, 10 mM HEPES, 35 mM sodium acetate pH 4.1, 2.2% (w/v) PEG 4000, 0.3 mM sulfonyl piperazine, 0.7% (v/v) DMSO, 22% (v/v) glycerol, and about 3-4 mM n-decyl-beta-D-thiomaltopyranoside
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F141H/L142S/L146S/F147H/E14A/E15A/K161T/E162A
solubilized enzyme version with 488% activity compared to the wild type enzyme, including four solubilizing mutations (F141H, L142S, L146S, and F147H) and four surface entropy reduction mutations (E14A, E15A, K161T, and E162A) to improve protein expression and crystallization
I47C/R149C
the mutant shows 141% activity compared to the wild type enzyme
I47G/R149G
the mutant shows 11.3% activity compared to the wild type enzyme
W136H
the mutant shows 600% activity compared to the wild type enzyme
H10N
the inactive mutant shows loss of manganese 1-binding ability
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Triton X-100
Triton X-100
while stimulated about 3fold in the presence of 0.05% (w/v) Triton X-100, the apparent activity does not decrease at high concentrations of Triton X-100
Triton X-100
-
while stimulated about 3fold in the presence of 0.05% (w/v) Triton X-100, the apparent activity does not decrease at high concentrations of Triton X-100
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
High-Trap Q Sepharose column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in E. coli strain BL21(DE3) and Bordetella pertussis strain B213
-
expressed in Escherichia coli BL21(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Babinski, K.J.; Ribeiro, A.A.; Raetz, C.R.
The Escherichia coli gene encoding the UDP-2,3-diacylglucosamine pyrophosphatase of lipid A biosynthesis
J. Biol. Chem.
277
25937-2546
2002
Escherichia coli (P43341), Escherichia coli
brenda
Babinski, K.J.; Kanjilal, S.J.; Raetz, C.R.
Accumulation of the lipid A precursor UDP-2,3-diacylglucosamine in an Escherichia coli mutant lacking the lpxH gene
J. Biol. Chem.
277
25947-25956
2002
Escherichia coli, Pseudomonas aeruginosa
brenda
Metzger, L.E.; Raetz, C.R.
An alternative route for UDP-diacylglucosamine hydrolysis in bacterial lipid A biosynthesis
Biochemistry
49
6715-6726
2010
Caulobacter vibrioides (A0A0H3C8Q1), Caulobacter vibrioides, Caulobacter vibrioides CB15 (A0A0H3C8Q1)
brenda
Dimou, M.; Venieraki, A.; Liakopoulos, G.; Kouri, E.D.; Tampakaki, A.; Katinakis, P.
Gene expression and biochemical characterization of Azotobacter vinelandii cyclophilins and protein interaction studies of the cytoplasmic isoform with dnaK and lpxH
J. Mol. Microbiol. Biotechnol.
20
176-190
2011
Azotobacter vinelandii (C1DHE3)
brenda
Young, H.E.; Donohue, M.P.; Smirnova, T.I.; Smirnov, A.I.; Zhou, P.
The UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis utilizes Mn2+ cluster for catalysis
J. Biol. Chem.
288
26987-27001
2013
Haemophilus influenzae (P44046), Haemophilus influenzae, Haemophilus influenzae DSM 11121 (P44046)
brenda
Lee, M.; Zhao, J.; Kwak, S.H.; Cho, J.; Lee, M.; Gillespie, R.A.; Kwon, D.Y.; Lee, H.; Park, H.J.; Wu, Q.; Zhou, P.; Hong, J.
Structure-activity relationship of sulfonyl piperazine LpxH inhibitors analyzed by an LpxE-coupled malachite green assay
ACS Infect. Dis.
5
641-651
2019
Escherichia coli
brenda
Bohl, T.; Ieong, P.; Lee, J.; Lee, T.; Kankanala, J.; Shi, K.; Demir, A.; Kurahashi, K.; Amaro, R.; Wang, Z.; Aihara, H.
The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release
J. Biol. Chem.
293
7969-7981
2018
Escherichia coli (P43341)
brenda
Arenas, J.; Pupo, E.; De Jonge, E.; Perez-Ortega, J.; Schaarschmidt, J.; Van Der Ley, P.; Tommassen, J.
Substrate specificity of the pyrophosphohydrolase LpxH determines the asymmetry of Bordetella pertussis lipid A
J. Biol. Chem.
294
7982-7989
2019
Neisseria meningitidis
brenda
Cho, J.; Lee, C.; Zhao, J.; Young, H.; Zhou, P.
Structure of the essential Haemophilus influenzae UDP-diacylglucosamine pyrophosphohydrolase LpxH in lipid A biosynthesis
Nat. Microbiol.
1
16154
2016
Haemophilus influenzae
brenda
Richie, D.; Takeoka, K.; Bojkovic, J.; Metzger, L.; Rath, C.; Sawyer, W.; Wei, J.; Dean, C.
Toxic accumulation of lps pathway intermediates underlies the requirement of LpxH for growth of acinetobacter Baumannii ATCC 19606
PLoS ONE
11
e0160918
2016
Acinetobacter baumannii, Acinetobacter baumannii (D0C652), Acinetobacter baumannii ATCC 19606, Acinetobacter baumannii ATCC 19606 (D0C652)
brenda
Okada, C.; Wakabayashi, H.; Kobayashi, M.; Shinoda, A.; Tanaka, I.; Yao, M.
Crystal structures of the UDP-diacylglucosamine pyrophosphohydrase LpxH from Pseudomonas aeruginosa
Sci. Rep.
6
32822
2016
Pseudomonas aeruginosa (Q9I2V0), Pseudomonas aeruginosa
brenda
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