Information on EC 3.6.1.27 - undecaprenyl-diphosphate phosphatase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
3.6.1.27
-
RECOMMENDED NAME
GeneOntology No.
undecaprenyl-diphosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
di-trans,poly-cis-undecaprenyl phosphate biosynthesis
-
-
peptidoglycan biosynthesis
-
-
Peptidoglycan biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
ditrans,octacis-undecaprenyl-diphosphate phosphohydrolase
Isolated from the bacteria Micrococcus lysodeikticus [1], Escherichia coli [2,3,5,6] and Bacillus subtilis [4]. The product of the reaction, ditrans,octacis-undecaprenyl phosphate, is essential for cell wall polysaccharide biosynthesis in these strains.
CAS REGISTRY NUMBER
COMMENTARY hide
9077-80-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
an undecaprenyl pyrophosphate phosphatase null mutant does not show any significant growth or morphological defect, neither is its sensitivity to bacitracin affected. However, the enzyme activity in the mutant is reduced by 75%
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
show the reaction diagram
diphosphate + H2O
2 phosphate
show the reaction diagram
-
low activity
-
-
?
diphosphate + H2O
phosphate + phosphate
show the reaction diagram
-
low activity
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
show the reaction diagram
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
show the reaction diagram
phosphatidic acid + H2O
?
show the reaction diagram
-
low activity
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
additional information
?
-
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
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
enhances inhibitory effect of bacitacin, slight inhibitory effect without bacitracin
Co2+
-
enhances inhibitory effect of bacitacin, slight inhibitory effect without bacitracin
Cu2+
-
enhances inhibitory effect of bacitacin
Fe2+
-
enhances inhibitory effect of bacitacin, slight inhibitory effect without bacitracin
Mn2+
-
enhances inhibitory effect of bacitacin, slight inhibitory effect without bacitracin
Zn2+
-
enhances inhibitory effect of bacitacin
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bacitracin
DTNB
-
slight inhibition
EDTA
-
5 mM, complete loss of activity
n-butanol
-
-
n-Propanol
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inhibitory at concentrations above 1.5 M
p-Chloromercuriphenylsulfonic acid
-
-
tetrahydrofuran
-
inhibitory at concentrations above 2 M
tripropeptin C
tripropeptin C can potentially inhibit C55-PP phosphatase activity, which plays a crucial role in the lipid cycle of peptidoglycan synthesis
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
-
-
diacylglycerol diphosphate
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increases the activity with undecaprenyl diphosphate by about 400%
ethanol
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slight activation at concentration of 4 M
methanol
-
slight activation at concentration of 4 M
n-Propanol
-
activating at concentrations below 1.5 M
phosphatidylglycerol
-
-
Phospholipids
-
-
Triton X-100
-
-
Triton X-114
-
-
additional information
-
significant rise in activity at high ionic strength
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.08
diacylglycerol diphosphate
-
pH 7.5, 37C, recombinant enzyme
3.9
diphosphate
-
pH 7.5, 37C, recombinant enzyme
0.0108 - 0.096
farnesyl diphosphate
3.6
isopentenyl diphosphate
-
pH 7.5, 37C, recombinant enzyme
1.7
phosphatidic acid
-
pH 7.5, 37C, recombinant enzyme
0.4 - 0.53
undecaprenyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
280
diacylglycerol diphosphate
Escherichia coli
-
pH 7.5, 37C, recombinant enzyme
48
diphosphate
Escherichia coli
-
pH 7.5, 37C, recombinant enzyme
2.1 - 290
farnesyl diphosphate
19
isopentenyl diphosphate
Escherichia coli
-
pH 7.5, 37C, recombinant enzyme
61
phosphatidic acid
Escherichia coli
-
pH 7.5, 37C, recombinant enzyme
9
undecaprenyl diphosphate
Escherichia coli
-
pH 7.5, 37C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0078
bacitracin
-
pH 7.0, 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
bacitracin
Escherichia coli
-
pH 7.0, 37C
0.00003 - 0.0001
tripropeptin C
Micrococcus luteus
C5CBT8
in 100 mM Tris-HCl, 10 mM MgCl2 and 3.9 mM n-dodecyl-beta-maltoside (pH 7.5), 1.25 mM CaCl2, at 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.198
-
non-purified
0.23
-
after first step of n-dodecyl-beta-D-maltoside extraction
0.73
-
purified His-tagged BcrC
1
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purified recombinant enzyme, substrate isopentenyl diphosphate
3
-
purified recombinant enzyme, substrate undecaprenyl diphosphate
6.7
-
purified recombinant enzyme, substrate phosphatidic acid
300
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purified recombinant enzyme, substrate farnesyl diphosphate
310
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purified recombinant enzyme, substrate diacylglycerol diphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7
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-
6.5 - 7.5
-
-
7.3 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
UppP accounts for 75% of the total cellular Und-PP pyrophosphatase activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
UppP and UppS exert their enzymic activity on the cytoplasmic side of the plasma membrane
Manually annotated by BRENDA team
additional information
-
topological mapping, modelling, overview
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
-
SDS-PAGE, His-tagged BcrC
110000
-
recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 17388, mass spectrometry
oligomer
-
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
additional information
-
the enzyme exists as a monomer in n-dodecyl-beta-D-maltoside solution, topological mapping, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
-
significant loss of activity by freezing and thawing one time
4
-
30-40% loss of activity within 1 week
25
-
solubilized enzyme stable for 30 min below 25C, loss of activity with higher temperatures
40
-
particular enzyme stable for 30 min below 40C, loss of activity with higher temperatures
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ascorbic acid stabilizes
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from membranes to homogeneity by ultracentrifugation, nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BWTs2bacA
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gene pgpB, overexpression of His-tagged enzyme in strain DH5alpha and C43
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of is constitutive and not affected by bacitracin or cell wall-active antimicrobials
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D111A
-
mutation in membrane-water interface, 100% residual activity
D150A
-
mutation in membrane-water interface, 64% residual activity
D43A
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mutation in aequous interface, 73% residual activity
E17A
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mutation within the consensus regions, 26% residiual activity
E17A/E21A
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mutation within the consensus regions, mutant is completely inactive
E194A
-
mutation in aequous interface, 31% residual activity
E21A
-
mutation within the consensus regions, 40% residiual activity
E41A
-
mutation in aequous interface, 85% residual activity
E49A
-
mutation in membrane-water interface, 36% residual activity
H30A
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mutation within the consensus regions, mutant is completely inactive
Q53A
-
mutation in membrane-water interface, 14% residual activity
R174A
-
mutation within the consensus regions, mutant is completely inactive
R189A
-
mutation in aequous interface, 11% residual activity
R261A
-
completely inactive
S173A
-
mutation within the consensus regions, mutant is completely inactive
S175A
-
mutation within the consensus regions, 32% residiual activity
T178A
-
mutation within the consensus regions, mutant is completely inactive
additional information
-
construction of chromosomal gene deletions mutants, double and triple deletion mutants in the genes uppP and ybjG, and uppP, ybjG and yeiU, respectively, are supersensitive to the Und-P de novo biosynthesis inhibitor fosmidomycin, while single or combined deletions including pgpB have no effect on fosmidomycin supersensitivity, overview
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