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Literature summary for 3.6.1.27 extracted from

  • 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 (2015), PLoS ONE, 10, e0142870 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Lauryldimethylamine oxide the enzyme shows optimal activity at 0.1% (v/v) lauryldimethylamine oxide (4.3 mM) Escherichia coli
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) Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli C43(DE3) cells Escherichia coli

Protein Variants

Protein Variants Comment Organism
E21A the mutant shows 1.4% of wild type activity Escherichia coli
H30A the mutant shows 6.2% of wild type activity Escherichia coli
Q164A the mutant shows 24.3% of wild type activity Escherichia coli
R174A the mutant shows 0.13% of wild type activity Escherichia coli
R189A the mutant shows 12.1% of wild type activity Escherichia coli
S173A the mutant shows 2.2% of wild type activity Escherichia coli
S175A the mutant shows 41% of wild type activity Escherichia coli
S196A the mutant shows 36.8% of wild type activity Escherichia coli
S26A the mutant shows 15% of wild type activity Escherichia coli
S27A the mutant shows 0.013% of wild type activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
EDTA 95% inhibition at 0.05 mM, 98% inhibition at 1 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.68
-
undecaprenyl diphosphate at pH 7.5 and 37°C Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
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 Escherichia coli
Mg2+ the enzyme activity lost after treatment with 0.05 mM EDTA is fully recovered following addition of Mg2+ (1 mM) Escherichia coli
Mn2+ the enzyme activity lost after treatment with 0.05 mM EDTA is partially recovered following addition of Mn2+ (1 mM) Escherichia coli
additional information no activity with Co2+, Fe2+, Zn2+, and Cu2+ Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
undecaprenyl diphosphate + H2O Escherichia coli
-
undecaprenyl phosphate + phosphate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and Superdex S200 gel filtration Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.5
-
with diacylglycerol diphosphate as substrate, at pH 7.5 and 37°C Escherichia coli
10.3
-
with farnesyl diphosphate as substrate, at pH 7.5 and 37°C Escherichia coli
11.3
-
with undecaprenyl diphosphate as substrate, at pH 7.5 and 37°C Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diacylglycerol diphosphate + H2O relatively good substrate Escherichia coli diacylglycerol phosphate + phosphate
-
?
farnesyl diphosphate + H2O
-
Escherichia coli farnesyl phosphate + phosphate
-
?
additional information no activity with isopentenyl diphosphate, phosphatidylglycerol phosphate and phosphatidic acid Escherichia coli ?
-
-
undecaprenyl diphosphate + H2O
-
Escherichia coli undecaprenyl phosphate + phosphate
-
?

Subunits

Subunits Comment Organism
? x * 25000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
bacA
-
Escherichia coli
C55-PP phosphatase
-
Escherichia coli
undecaprenyl-pyrophosphate phosphatase
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65 70 the enzyme has optimal activity at 65-70°C which is about 16 fold higher than at 37°C Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
73.5
-
melting temperature Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
27
-
undecaprenyl diphosphate at pH 7.5 and 37°C Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
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 Escherichia coli