Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.6.1.27 - undecaprenyl-diphosphate phosphatase and Organism(s) Escherichia coli and UniProt Accession P60932

for references in articles please use BRENDA:EC3.6.1.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
Isolated from the bacteria Micrococcus lysodeikticus , Escherichia coli [2,3,5,6] and Bacillus subtilis . The product of the reaction, ditrans,octacis-undecaprenyl phosphate, is essential for cell wall polysaccharide biosynthesis in these strains.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P60932
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
undecaprenyl pyrophosphate phosphatase, upp phosphatase, smu.244, c55-pp phosphatase, undecaprenyl diphosphate phosphatase, c55-pp pyrophosphatase, hp0851, undecaprenyl pyrophosphatase, undecaprenyl-diphosphate phosphatase, undecaprenyl-pyrophosphate phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Und-pp phosphatase
-
undecaprenyl pyrophosphate phosphatase
-
undecaprenyl-pyrophosphate phosphatase
-
C55-isoprenyl diphosphatase
-
-
-
-
C55-isoprenyl pyrophosphatase
-
-
-
-
C55-PP phosphatase
-
-
Dolicholpyrophosphatase
-
-
-
-
isoprenyl pyrophosphatase
-
-
-
-
undecaprenyl diphosphate phosphatase
-
-
undecaprenyl pyrophosphate phosphatase
-
-
undecaprenyl-pyrophosphate phosphatase
-
-
UPP phosphatase
-
-
additional information
-
the enzyme is a member of the type 2 phosphatidic acid phosphatase family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
farnesyl diphosphate + H2O
farnesyl phosphate + phosphate
show the reaction diagram
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + 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
-
-
?
ditrans,octacis-undecaprenyl diphosphate + H2O
ditrans,octacis-undecaprenyl 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
additional information
?
-
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
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
?
ditrans,octacis-undecaprenyl diphosphate + H2O
ditrans,octacis-undecaprenyl phosphate + phosphate
show the reaction diagram
-
-
-
-
?
undecaprenyl diphosphate + H2O
undecaprenyl phosphate + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
or Ca2+, absolutely required
Ca2+
-
the enzyme activity lost after treatment with 0.05 mM EDTA is not only fully recovered following addition of Ca2+ (1 mM) but also greatly enhanced by an about 9fold factor
Mg2+
-
the enzyme activity lost after treatment with 0.05 mM EDTA is fully recovered following addition of Mg2+ (1 mM)
Mn2+
-
the enzyme activity lost after treatment with 0.05 mM EDTA is partially recovered following addition of Mn2+ (1 mM)
additional information
-
no activity with Co2+, Fe2+, Zn2+, and Cu2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
5 mM, complete loss of activity
(5-bromo-2-[[3-(octyloxy)phenyl]methoxy]phenyl)phosphonic acid
-
-
2-(N-methyl-3-(octyloxy)benzamido)phenylphosphonic acid
-
-
2-methoxy-6-[3-(octyloxy)benzamido]benzoic acid
-
-
2-[3,4-bis(2-methoxyethoxy)benzamido]-5-bromobenzoic acid
-
-
2-[3-(hexyloxy)benzamido]benzoic acid
-
-
2-[3-(octyloxy)benzamido]-5-(trifluoromethoxy)benzoic acid
2-[3-(octyloxy)benzamido]-5-phosphonobenzoic acid
-
-
2-[3-(octyloxy)benzamido]benzoic acid
-
-
2-[methyl[3-(octyloxy)benzoyl]amino]benzoic acid
-
-
3,4,5-trimethoxy-2-[3-(octyloxy)benzamido]benzoic acid
-
-
3-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
3-[3-(hexyloxy)benzamido]-4-hydroxybenzoic acid
-
-
3-[3-(octyloxy)benzamido]benzene-1,2-dicarboxylic acid
-
-
3-[3-(octyloxy)benzamido]benzoic acid
-
-
4,5-difluoro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
4-hydroxy-3-[3-(octyloxy)benzamido]benzoic acid
-
-
4-[3-(octyloxy)benzamido]benzene-1,3-dicarboxylic acid
-
-
5-(diethoxyphosphoryl)-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-(methanesulfonyl)-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-bromo-2-[3-(3,3-dimethylbut-1-yn-1-yl)benzamido]benzoic acid
-
-
5-bromo-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-chloro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-fluoro-2-(3-(octyloxy)benzamido)benzoic acid
-
-
5-fluoro-2-[3-(hexyloxy)benzamido]benzoic acid
-
-
5-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-hydroxy-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-methoxy-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-methoxy-4-(2-methoxyethoxy)-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-nitro-2-[3-(octyloxy)benzamido]benzoic acid
-
-
5-[3-(octyloxy)benzamido]benzene-1,3-dicarboxylic acid
-
-
bacitracin
-
-
EDTA
-
95% inhibition at 0.05 mM, 98% inhibition at 1 mM
N-(2-carbamoylphenyl)-3-(octyloxy)benzamide
-
-
[2-[3-(octyloxy)benzamido]phenyl]phosphonic acid
-
-
[3-[3-(octyloxy)benzamido]phenyl]phosphonic acid
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cardiolipin
-
-
diacylglycerol diphosphate
-
increases the activity with undecaprenyl diphosphate by about 400%
Lauryldimethylamine oxide
-
the enzyme shows optimal activity at 0.1% (v/v) lauryldimethylamine oxide (4.3 mM)
n-dodecyl-beta-D-maltopyranoside
-
the enzyme activity appears optimal at low n-dodecyl-beta-D-maltopyranoside concentrations around 0.050-15% (v/v) (1-3 mM)
phosphatidylglycerol
-
-
Phospholipids
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0108
farnesyl diphosphate
wild-type, pH 7.0, 37°C
0.08
diacylglycerol diphosphate
-
pH 7.5, 37°C, recombinant enzyme
3.9
diphosphate
-
pH 7.5, 37°C, recombinant enzyme
0.096
farnesyl diphosphate
-
pH 7.5, 37°C, recombinant enzyme
3.6
isopentenyl diphosphate
-
pH 7.5, 37°C, recombinant enzyme
1.7
phosphatidic acid
-
pH 7.5, 37°C, recombinant enzyme
0.53 - 0.68
undecaprenyl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
farnesyl diphosphate
wild-type, pH 7.0, 37°C
280
diacylglycerol diphosphate
-
pH 7.5, 37°C, recombinant enzyme
48
diphosphate
-
pH 7.5, 37°C, recombinant enzyme
290
farnesyl diphosphate
-
pH 7.5, 37°C, recombinant enzyme
19
isopentenyl diphosphate
-
pH 7.5, 37°C, recombinant enzyme
61
phosphatidic acid
-
pH 7.5, 37°C, recombinant enzyme
9 - 27
undecaprenyl diphosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0078
bacitracin
pH 7.0, 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.033
bacitracin
Escherichia coli
pH 7.0, 37°C
0.0067
(5-bromo-2-[[3-(octyloxy)phenyl]methoxy]phenyl)phosphonic acid
0.0065
2-(N-methyl-3-(octyloxy)benzamido)phenylphosphonic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.2
2-methoxy-6-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.2
2-[3,4-bis(2-methoxyethoxy)benzamido]-5-bromobenzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.045
2-[3-(hexyloxy)benzamido]benzoic acid
0.00083
2-[3-(octyloxy)benzamido]-5-(trifluoromethoxy)benzoic acid
0.0042
2-[3-(octyloxy)benzamido]-5-phosphonobenzoic acid
0.01
2-[3-(octyloxy)benzamido]benzoic acid
0.2
2-[methyl[3-(octyloxy)benzoyl]amino]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.2
3,4,5-trimethoxy-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0085
3-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.031
3-[3-(hexyloxy)benzamido]-4-hydroxybenzoic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.2
3-[3-(octyloxy)benzamido]benzene-1,2-dicarboxylic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.073
3-[3-(octyloxy)benzamido]benzoic acid
0.0034
4,5-difluoro-2-[3-(octyloxy)benzamido]benzoic acid
0.031
4-hydroxy-3-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.2
4-[3-(octyloxy)benzamido]benzene-1,3-dicarboxylic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0085 - 0.2
5-(diethoxyphosphoryl)-2-[3-(octyloxy)benzamido]benzoic acid
0.0098
5-(methanesulfonyl)-2-[3-(octyloxy)benzamido]benzoic acid
0.2
5-bromo-2-[3-(3,3-dimethylbut-1-yn-1-yl)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0042
5-bromo-2-[3-(octyloxy)benzamido]benzoic acid
0.003
5-chloro-2-[3-(octyloxy)benzamido]benzoic acid
0.0027
5-fluoro-2-(3-(octyloxy)benzamido)benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.02
5-fluoro-2-[3-(hexyloxy)benzamido]benzoic acid
0.0013 - 0.0027
5-fluoro-2-[3-(octyloxy)benzamido]benzoic acid
0.011
5-hydroxy-2-[3-(octyloxy)benzamido]benzoic acid
0.2
5-methoxy-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.2
5-methoxy-4-(2-methoxyethoxy)-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0013
5-nitro-2-[3-(octyloxy)benzamido]benzoic acid
Escherichia coli
-
at pH 7.5 and 20°C
0.2
5-[3-(octyloxy)benzamido]benzene-1,3-dicarboxylic acid
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.032
bacitracin
0.2
N-(2-carbamoylphenyl)-3-(octyloxy)benzamide
Escherichia coli
-
IC50 above 0.2 mM, at pH 7.5 and 20°C
0.0065
[2-[3-(octyloxy)benzamido]phenyl]phosphonic acid
Escherichia coli
-
pH and temperature not specified in the publication, mutant enzyme Y246D
0.0071
[3-[3-(octyloxy)benzamido]phenyl]phosphonic acid
Escherichia coli
-
at pH 7.5 and 20°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
-
purified recombinant enzyme, substrate isopentenyl diphosphate
10.3
-
with farnesyl diphosphate as substrate, at pH 7.5 and 37°C
11.3
-
with undecaprenyl diphosphate as substrate, at pH 7.5 and 37°C
3
-
purified recombinant enzyme, substrate undecaprenyl diphosphate
300
-
purified recombinant enzyme, substrate farnesyl diphosphate
310
-
purified recombinant enzyme, substrate diacylglycerol diphosphate
5.5
-
with diacylglycerol diphosphate as substrate, at pH 7.5 and 37°C
6.7
-
purified recombinant enzyme, substrate phosphatidic acid
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7.5
-
a plateau of maximal activity is observed between 5.0 and 7.5. The enzyme does not show significant activity at acid pH values below 5.0
6.5 - 7.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
50% of maximal activity at pH values other than pH 6.5-pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
65 - 70
-
the enzyme has optimal activity at 65-70°C which is about 16 fold higher than at 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
-
Manually annotated by BRENDA team
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%
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17388
x * 17388, mass spectrometry
110000
-
recombinant His-tagged enzyme, gel filtration
30000
-
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
30158
-
x * 30158, mass spectrometry, x * 30000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 17388, mass spectrometry
?
-
x * 25000, SDS-PAGE
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using 40% (w/v) PEG 400, 0.3-0.5M ammonium citrate dibasic and 0.1M sodium citrate pH 5.0
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D111A
mutation in membrane-water interface, 100% residual activity
D150A
mutation in membrane-water interface, 64% residual activity
D43A
mutation in aequous interface, 73% residual activity
E17A
mutation within the consensus regions, 26% residiual activity
E17A/E21A
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
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
E21A
-
the mutant shows 1.4% of wild type activity
H30A
-
the mutant shows 6.2% of wild type activity
Q164A
-
the mutant shows 24.3% of wild type activity
R174A
-
the mutant shows 0.13% of wild type activity
R189A
-
the mutant shows 12.1% of wild type activity
S173A
-
the mutant shows 2.2% of wild type activity
S175A
-
the mutant shows 41% of wild type activity
S196A
-
the mutant shows 36.8% of wild type activity
S26A
-
the mutant shows 15% of wild type activity
S27A
-
the mutant shows 0.013% of wild type activity
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
73.5
-
melting temperature
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Superdex S200 gel filtration
Ni-NTA column chromatography and Superdex S200 gel filtration
-
recombinant His-tagged enzyme from membranes to homogeneity by ultracentrifugation, nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C43(DE3) cells
expressed in Escherichia coli C43(DE3) cells
-
gene pgpB, overexpression of His-tagged enzyme in strain DH5alpha and C43
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pharmacology
-
the enzyme is an attractive drug target since it is not used by humans
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
El Ghachi, M.; Derbise, A.; Bouhss, A.; Mengin-Lecreulx, D.
Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli
J. Biol. Chem.
280
18689-18695
2005
Escherichia coli
Manually annotated by BRENDA team
Touze, T.; Blanot, D.; Mengin-Lecreulx, D.
Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase
J. Biol. Chem.
283
16573-16583
2008
Escherichia coli
Manually annotated by BRENDA team
Tatar, L.D.; Marolda, C.L.; Polischuk, A.N.; van Leeuwen, D.; Valvano, M.A.
An Escherichia coli undecaprenyl-pyrophosphate phosphatase implicated in undecaprenyl phosphate recycling
Microbiology
153
2518-2529
2007
Escherichia coli
Manually annotated by BRENDA team
Coker, O.; Palittapongarnpim, P.
Current understanding of de novo synthesis of bacterial lipid carrier (undecaprenyl phosphate): More enzymes to be discovered
Afr. J. Microbiol. Res.
5
2555-2565
2011
Escherichia coli (P60932), Bacillus subtilis (P94571)
-
Manually annotated by BRENDA team
Chang, H.Y.; Chou, C.C.; Hsu, M.F.; Wang, A.H.
Proposed carrier lipid-binding site of undecaprenyl pyrophosphate phosphatase from Escherichia coli
J. Biol. Chem.
289
18719-18735
2014
Escherichia coli (P60932), Escherichia coli
Manually annotated by BRENDA team
Kawakami, N.; Fujisaki, S.
Undecaprenyl phosphate metabolism in Gram-negative and Gram-positive bacteria
Biosci. Biotechnol. Biochem.
82
940-946
2018
Escherichia coli
Manually annotated by BRENDA team
Wang, Y.; Desai, J.; Zhang, Y.; Malwal, S.R.; Shin, C.J.; Feng, X.; Sun, H.; Liu, G.; Guo, R.T.; Oldfield, E.
Bacterial cell growth inhibitors targeting undecaprenyl diphosphate synthase and undecaprenyl diphosphate phosphatase
ChemMedChem
11
2311-2319
2016
Escherichia coli
Manually annotated by BRENDA team
El Ghachi, M.; Howe, N.; Huang, C.Y.; Olieric, V.; Warshamanage, R.; Touze, T.; Weichert, D.; Stansfeld, P.J.; Wang, M.; Kerff, F.; Caffrey, M.
Crystal structure of undecaprenyl-pyrophosphate phosphatase and its role in peptidoglycan biosynthesis
Nat. Commun.
9
1078
2018
Escherichia coli (P60932)
Manually annotated by BRENDA team
Manat, G.; El Ghachi, M.; Auger, R.; Baouche, K.; Olatunji, S.; Kerff, F.; Touze, T.; Mengin-Lecreulx, D.; Bouhss, A.
Membrane topology and biochemical characterization of the Escherichia coli BacA undecaprenyl-pyrophosphate phosphatase
PLoS ONE
10
e0142870
2015
Escherichia coli
Manually annotated by BRENDA team