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
3.6.1.27
-
RECOMMENDED NAME
GeneOntology No.
undecaprenyl-diphosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ditrans,octacis-undecaprenyl diphosphate + H2O = ditrans,octacis-undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
bacA
P60932
gene name
BcrC
-
formerly YwoA
BcrC
P94571
-
C55-isoprenyl diphosphatase
-
-
-
-
C55-isoprenyl pyrophosphatase
-
-
-
-
C55-PP phosphatase
-
-
C55-PP phosphatase
-
-
-
C55-PP phosphatase
C5CBT8
-
Dolicholpyrophosphatase
-
-
-
-
Und-pp phosphatase
P94571
-
Und-pp phosphatase
P60932
-
undecaprenyl pyrophosphate phosphatase
-
-
undecaprenyl pyrophosphate phosphatase
P94571
-
undecaprenyl pyrophosphate phosphatase
-
-
undecaprenyl pyrophosphate phosphatase
-
-
-
undecaprenyl pyrophosphate phosphatase
-
-
undecaprenyl pyrophosphate phosphatase
P60932
-
undecaprenyl pyrophosphate phosphatase
C5CBT8
-
undecaprenyl-pyrophosphate phosphatase
-
-
Upp-P
P94571
-
Upp-P
P60932
-
UppP
-
formerly BacA
UppP
C5CBT8
-
isoprenyl pyrophosphatase
-
-
-
-
additional information
-
the enzyme is a member of the type 2 phosphatidic acid phosphatase family
CAS REGISTRY NUMBER
COMMENTARY
9077-80-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
genes uppP, ybjG, and yeiU
-
-
Manually annotated by BRENDA team
strains DH5alpha, JM83 and C43(DE3)
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
P60932
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
P94571
the enzyme confers resistance to bacitracin
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
low activity
-
-
?
diacylglycerol diphosphate + H2O
diacylglycerol phosphate + phosphate
show the reaction diagram
-
-
-
-
?
diacylglycerol diphosphate + H2O
diaclyglycerol phosphate + phosphate
show the reaction diagram
-
low activity
-
-
?
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
-
-
-
-
?
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
show the reaction diagram
-
-
-
-
?
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
show the reaction diagram
-
low activity
-
-
?
phosphatidic acid + H2O
?
show the reaction diagram
-
low activity
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
P94571
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
P60932
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
low activity
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
involved in cyclic peptidoglycan pathway
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
involved in cyclic peptidoglycan pathway
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
the dephosphorylation of Und-PP, from de novo synthesis, produces undecaprenyl phosphate, a universal lipid carrier of glycan biosynthetic intermediates for carbohydrate polymers that are exported to the bacterial cell envelope, YbjG and YeiU are implicated in the recycling of periplasmic Und-PP molecules
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
the synthesis of the lipid carrier undecaprenyl phosphate, C55-P, requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate, C55-PP, the dephosphorylation involves four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG, and YeiU, overview
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
-
?
isopentenyl diphosphate + H2O
isopentenyl phosphate + phosphate
show the reaction diagram
-
low activity
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
undecaprenyl phosphate is no substrate, no activity on monophosphate compounds is observed. PbrB cannot dephosphorylate phosphatidic acid or glucose-6-phosphate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
involved in cyclic peptidoglycan pathway
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
involved in cyclic peptidoglycan pathway
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
the dephosphorylation of Und-PP, from de novo synthesis, produces undecaprenyl phosphate, a universal lipid carrier of glycan biosynthetic intermediates for carbohydrate polymers that are exported to the bacterial cell envelope, YbjG and YeiU are implicated in the recycling of periplasmic Und-PP molecules
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
the synthesis of the lipid carrier undecaprenyl phosphate, C55-P, requires the dephosphorylation of its precursor, undecaprenyl pyrophosphate, C55-PP, the dephosphorylation involves four integral membrane proteins, BacA, and three members of the type 2 phosphatidic acid phosphatase family, PgpB, YbjG, and YeiU, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
enhances inhibitory effect of bacitacin
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
Mg2+
-
enhances inhibitory effect of bacitacin
Zn2+
-
enhances inhibitory effect of bacitacin
Mn2+
-
enhances inhibitory effect of bacitacin, slight inhibitory effect without bacitracin
additional information
-
no requirement for added metal ions
additional information
-
no requirement for added metal ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Bacitracin
-
complex formation with substrate + metal ion, reversed by addition of chelating agents
Bacitracin
-
partial inhibition at 10 mM bacitracin
Bacitracin
C5CBT8
-
n-Propanol
-
inhibitory at concentrations above 1.5 M
p-Chloromercuriphenylsulfonic acid
-
-
tetrahydrofuran
-
inhibitory at concentrations above 2 M
tripropeptin C
C5CBT8
tripropeptin C can potentially inhibit C55-PP phosphatase activity, which plays a crucial role in the lipid cycle of peptidoglycan synthesis
-
DTNB
-
slight inhibition
additional information
-
no inhibitory effect by reserpine
-
additional information
-
the enzyme is not inhibited by Pb2+ (0.0001-10 mM)
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cardiolipin
-
-
diacylglycerol diphosphate
-
increases the activity with undecaprenyl diphosphate by about 400%
ethanol
-
slight activation at concentration of 4 M
n-Propanol
-
activating at concentrations below 1.5 M
phosphatidylglycerol
-
-
Phospholipids
-
-
methanol
-
slight activation at concentration of 4 M
additional information
-
significant rise in activity at high ionic strength
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.08
-
diacylglycerol diphosphate
-
pH 7.5, 37C, recombinant enzyme
3.9
-
diphosphate
-
pH 7.5, 37C, recombinant enzyme
0.096
-
farnesyl diphosphate
-
pH 7.5, 37C, recombinant enzyme
3.6
-
isopentenyl diphosphate
-
pH 7.5, 37C, recombinant enzyme
1.7
-
phosphatidic acid
-
pH 7.5, 37C, recombinant enzyme
0.4
-
undecaprenyl diphosphate
-
-
0.53
-
undecaprenyl diphosphate
-
pH 7.5, 37C, recombinant enzyme
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
280
-
diacylglycerol diphosphate
-
pH 7.5, 37C, recombinant enzyme
48
-
diphosphate
-
pH 7.5, 37C, recombinant enzyme
290
-
farnesyl diphosphate
-
pH 7.5, 37C, recombinant enzyme
19
-
isopentenyl diphosphate
-
pH 7.5, 37C, recombinant enzyme
61
-
phosphatidic acid
-
pH 7.5, 37C, recombinant enzyme
9
-
undecaprenyl diphosphate
-
pH 7.5, 37C, recombinant enzyme
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00003
0.0001
tripropeptin C
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.198
-
-
non-purified
0.23
-
-
after first step of n-dodecyl-beta-D-maltoside extraction
0.73
-
-
purified His-tagged BcrC
1
-
-
purified recombinant enzyme, substrate isopentenyl diphosphate
3
-
-
purified recombinant enzyme, substrate undecaprenyl diphosphate
6.7
-
-
purified recombinant enzyme, substrate phosphatidic acid
300
-
-
purified recombinant enzyme, substrate farnesyl diphosphate
310
-
-
purified recombinant enzyme, substrate diacylglycerol diphosphate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
9
-
50% of maximal activity at pH values other than pH 6.5-pH 7.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
UppP accounts for 75% of the total cellular Und-PP pyrophosphatase activity
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
UppP and UppS exert their enzymic activity on the cytoplasmic side of the plasma membrane
Manually annotated by BRENDA team
-
integral, PgpB contains six transmembrane segments, a large periplasmic loop, and the type 2 phosphatidic acid phosphatase signature residues at a periplasmic location
Manually annotated by BRENDA team
P94571
inner cytoplasmic membrane
Manually annotated by BRENDA team
P60932
inner cytoplasmic membrane
Manually annotated by BRENDA team
-
PgpB contains six transmembrane segments, a large periplasmic loop, and the type 2 phosphatidic acid phosphatase signature residues at a periplasmic location
-
Manually annotated by BRENDA team
-
YbjG and, to a lesser extent, YeiU exert their enzymic activity on the periplasmic side of the plasma membrane
-
Manually annotated by BRENDA team
additional information
-
topological mapping, modelling, overview
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22000
-
-
SDS-PAGE, His-tagged BcrC
110000
-
-
recombinant His-tagged enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
ascorbic acid stabilizes
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His-tagged enzyme from membranes to homogeneity by ultracentrifugation, nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli strain BWTs2bacA
-
gene pgpB, overexpression of His-tagged enzyme in strain DH5alpha and C43
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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