Information on EC 3.6.1.54 - UDP-2,3-diacylglucosamine diphosphatase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.6.1.54
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RECOMMENDED NAME
GeneOntology No.
UDP-2,3-diacylglucosamine diphosphatase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
lipid IVA biosynthesis
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lipid A biosynthesis
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Lipopolysaccharide biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
UDP-2,3-bis[(3R)-3-hydroxymyristoyl]-alpha-D-glucosamine 2,3-bis[(3R)-3-hydroxymyristoyl]-beta-D-glucosaminyl 1-phosphate phosphohydrolase
The enzyme catalyses a step in the biosynthesis of lipid A.
CAS REGISTRY NUMBER
COMMENTARY hide
469863-59-0
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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B8GWR0
UniProt
Manually annotated by BRENDA team
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B8GWR0
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
UDP-2,3-diacylglucosamine + H2O
2,3-diacylglucosamine 1-phosphate + UMP
show the reaction diagram
UDP-N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + H2O
N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine 1-phosphate + UMP
show the reaction diagram
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
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
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
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
10-50fold stimulation compared to conditions without metal additive
Mg2+
B8GWR0;
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+
Ni2+
10-50fold stimulation compared to conditions without metal additive
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
B8GWR0;
complete inhibition at 2 or 0.2 mM
Triton X-100
0.01%
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0079 - 0.105
UDP-2,3-diacylglucosamine
0.0617
UDP-N2,O3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine
pH 8.0, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
pH 8.0, 30°C
25
B8GWR0;
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
B8GWR0;
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 9
B8GWR0;
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
pH 6.5: about 50% of maximal activity, pH 9.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Caulobacter vibrioides (strain NA1000 / CB15N);
P43341
Escherichia coli (strain K12);
P44046
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd);
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26893
x * 26893, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 26893, calculated from sequence
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
High-Trap Q Sepharose column chromatography and Superdex 200 gel filtration
B8GWR0;
Ni-NTA column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21 (DE3) cells
expressed in lpxh-deficient Escherichia coli CcI 21b cells
B8GWR0;
lpxH overexpression is toxic to cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D117A
2fold decrease in activity compared to wild-type
D42A
80000fold decrease in activity compared to wild-type
D9A
200000fold decrease in activity compared to wild-type
H115A
12000fold decrease in activity compared to wild-type
H11A
20000fold decrease in activity compared to wild-type
H196A
5000fold decrease in activity compared to wild-type
R81A
7000fold decrease in activity compared to wild-type
D117A
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2fold decrease in activity compared to wild-type
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D42A
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80000fold decrease in activity compared to wild-type
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H115A
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12000fold decrease in activity compared to wild-type
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H11A
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20000fold decrease in activity compared to wild-type
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H196A
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5000fold decrease in activity compared to wild-type
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